SitesBLAST
Comparing 349652 FitnessBrowser__Btheta:349652 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
8a5eA Cryo-em structure of the electron bifurcating fe-fe hydrogenase hydabc complex from acetobacterium woodii in the reduced state (see paper)
48% identity, 99% coverage: 4:585/588 of query aligns to 2:579/583 of 8a5eA
- binding fe2/s2 (inorganic) cluster: T34 (= T36), C36 (= C38), G45 (≠ A52), C47 (= C54), C50 (= C57), C64 (= C71)
- binding 2 iron/2 sulfur/5 carbonyl/2 water inorganic cluster: C300 (= C313), P325 (= P338), M354 (= M367), C356 (= C369), K359 (= K372), C506 (= C517)
- binding iron/sulfur cluster: H96 (= H103), N97 (≠ P104), C100 (= C107), C103 (= C110), S106 (≠ C113), C109 (= C116), C148 (= C155), C151 (= C158), K152 (≠ R159), C154 (= C161), C158 (= C165), V166 (≠ A173), C191 (= C198), C194 (= C201), G195 (= G202), C197 (= C204), C201 (= C208), P202 (= P209), V203 (= V210), S301 (≠ C314), C356 (= C369), C502 (= C513), C506 (= C517)
8a6tA Cryo-em structure of the electron bifurcating fe-fe hydrogenase hydabc complex from thermoanaerobacter kivui in the reduced state (see paper)
48% identity, 99% coverage: 6:586/588 of query aligns to 4:568/571 of 8a6tA
- binding fe2/s2 (inorganic) cluster: C36 (= C38), D37 (≠ H39), C47 (= C54), R48 (= R55), C50 (= C57), C63 (= C71)
- binding 2 iron/2 sulfur/5 carbonyl/2 water inorganic cluster: A229 (= A238), P230 (= P239), A231 (= A240), C298 (= C313), P323 (= P338), M352 (= M367), P353 (= P368), K357 (= K372), F412 (= F431), C500 (= C517)
- binding iron/sulfur cluster: H95 (= H103), C99 (= C107), C102 (= C110), C108 (= C116), C146 (= C155), C149 (= C158), G150 (≠ R159), K151 (≠ R160), C152 (= C161), C156 (= C165), C189 (= C198), C192 (= C201), C195 (= C204), C199 (= C208), G202 (= G211), C299 (= C314), C354 (= C369), C496 (= C513), C500 (= C517)
5bysA Semisynthetic [fefe]-hydrogenase cpi with sulfur-dithiolato-bridged [2fe] cofactor (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 2:571/576 of 5bysA
- active site: E278 (= E287), E281 (= E290), C298 (= C313), S318 (= S333), K357 (= K372), E360 (= E375), Q365 (≠ E380), C502 (= C517)
- binding bis(cyanido-kappaC)(dicarbonyl)-mu-(oxomethylidene)-mu-(sulfanediyldimethanethiolatato-1kappaS:2kappaS)diiron(2+): A229 (= A238), P230 (= P239), S231 (≠ A240), I267 (≠ T276), C298 (= C313), P323 (= P338), Q324 (= Q339), M352 (= M367), P353 (= P368), K357 (= K372), F416 (= F431), V422 (= V437), M496 (= M511), C502 (= C517)
- binding fe2/s2 (inorganic) cluster: A31 (≠ T36), C33 (= C38), F34 (≠ H39), C45 (= C54), E46 (≠ R55), C48 (= C57), C61 (= C71)
- binding magnesium ion: N39 (≠ K48), D41 (≠ N50)
- binding iron/sulfur cluster: H93 (= H103), F95 (≠ N105), K96 (≠ D106), C97 (= C107), C100 (= C110), C106 (= C116), K145 (= K154), C146 (= C155), L147 (≠ I156), L148 (≠ F157), C149 (= C158), G150 (≠ R159), C152 (= C161), C156 (= C165), T160 (≠ Q169), A164 (= A173), M165 (≠ L174), I176 (= I185), C189 (= C198), L190 (≠ T199), L191 (≠ Y200), C192 (= C201), G193 (= G202), C195 (= C204), C199 (= C208), P200 (= P209), V201 (= V210), A202 (≠ G211), A203 (= A212), L204 (= L213), C299 (= C314), C354 (= C369), M496 (= M511), A497 (= A512), C498 (= C513), C502 (= C517)
6h63A Semisynthetic [fefe]-hydrogenase cpi with ethanedithiolate [2fe] cofactor
38% identity, 98% coverage: 7:582/588 of query aligns to 2:571/578 of 6h63A
- active site: E278 (= E287), E281 (= E290), C298 (= C313), S318 (= S333), K357 (= K372), E360 (= E375), Q365 (≠ E380), C502 (= C517)
- binding fe2/s2 (inorganic) cluster: C33 (= C38), F34 (≠ H39), C45 (= C54), E46 (≠ R55), C48 (= C57), C61 (= C71)
- binding dicarbonyl[bis(cyanide-kappaC)]-mu-(ethanethiolatato-1kappaS:2kappaS)-mu-(ox omethylidene)diiron(2+): A229 (= A238), P230 (= P239), S231 (≠ A240), C298 (= C313), P323 (= P338), Q324 (= Q339), M352 (= M367), P353 (= P368), K357 (= K372), F416 (= F431), M496 (= M511), C502 (= C517)
- binding magnesium ion: N39 (≠ K48), D41 (≠ N50)
- binding iron/sulfur cluster: H93 (= H103), F95 (≠ N105), K96 (≠ D106), C97 (= C107), C100 (= C110), R102 (≠ K112), C106 (= C116), C146 (= C155), L147 (≠ I156), L148 (≠ F157), C149 (= C158), G150 (≠ R159), C152 (= C161), C156 (= C165), T160 (≠ Q169), A164 (= A173), M165 (≠ L174), I176 (= I185), C189 (= C198), L190 (≠ T199), L191 (≠ Y200), C192 (= C201), G193 (= G202), C195 (= C204), C199 (= C208), P200 (= P209), V201 (= V210), A203 (= A212), L204 (= L213), C299 (= C314), C354 (= C369), A497 (= A512), C498 (= C513), C502 (= C517)
8aj6A Cyanide-bound [fefe]-hydrogenase i from clostridium pasteurianum (cpi) (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 3:572/580 of 8aj6A
- binding fe2/s2 (inorganic) cluster: A32 (≠ T36), C34 (= C38), F35 (≠ H39), C46 (= C54), E47 (≠ R55), C49 (= C57), C62 (= C71)
- binding magnesium ion: N40 (≠ K48), D42 (≠ N50)
- binding iron/sulfur cluster: H94 (= H103), F96 (≠ N105), K97 (≠ D106), C98 (= C107), C101 (= C110), R104 (≠ C113), C107 (= C116), C147 (= C155), L148 (≠ I156), L149 (≠ F157), C150 (= C158), G151 (≠ R159), C153 (= C161), C157 (= C165), T161 (≠ Q169), M166 (≠ L174), I177 (= I185), C190 (= C198), L191 (≠ T199), L192 (≠ Y200), C193 (= C201), G194 (= G202), C196 (= C204), C200 (= C208), P201 (= P209), V202 (= V210), A204 (= A212), L205 (= L213), C300 (= C314), C355 (= C369), A498 (= A512), C499 (= C513), C503 (= C517)
- binding Binuclear [FeFe], di(thiomethyl)amine, carbon monoxide, cyanide cluster (-CN form): A230 (= A238), P231 (= P239), S232 (≠ A240), C299 (= C313), P324 (= P338), Q325 (= Q339), M353 (= M367), P354 (= P368), K358 (= K372), F417 (= F431), M497 (= M511), C503 (= C517)
5byqA Semisynthetic [fefe]-hydrogenase cpi with oxodithiolato-bridged [2fe] cofactor (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 2:571/580 of 5byqA
- active site: E278 (= E287), E281 (= E290), C298 (= C313), S318 (= S333), K357 (= K372), E360 (= E375), Q365 (≠ E380), C502 (= C517)
- binding bis(cyanido-kappaC)(dicarbonyl)-mu-(oxomethylidene)-mu-(oxydimethanethiolate-1kappaS:2kappaS)diiron(2+): A229 (= A238), P230 (= P239), S231 (≠ A240), C298 (= C313), P323 (= P338), Q324 (= Q339), M352 (= M367), P353 (= P368), K357 (= K372), F416 (= F431), M496 (= M511), C502 (= C517)
- binding fe2/s2 (inorganic) cluster: A31 (≠ T36), C33 (= C38), F34 (≠ H39), C45 (= C54), E46 (≠ R55), C48 (= C57), C61 (= C71)
- binding magnesium ion: N39 (≠ K48), D41 (≠ N50)
- binding iron/sulfur cluster: H93 (= H103), F95 (≠ N105), K96 (≠ D106), C97 (= C107), C100 (= C110), R103 (≠ C113), C106 (= C116), K145 (= K154), C146 (= C155), L147 (≠ I156), L148 (≠ F157), C149 (= C158), G150 (≠ R159), C152 (= C161), C156 (= C165), T160 (≠ Q169), A164 (= A173), M165 (≠ L174), I176 (= I185), C189 (= C198), L190 (≠ T199), L191 (≠ Y200), C192 (= C201), G193 (= G202), Q194 (= Q203), C195 (= C204), C199 (= C208), P200 (= P209), V201 (= V210), A203 (= A212), L204 (= L213), C299 (= C314), C354 (= C369), M496 (= M511), A497 (= A512), C498 (= C513), C502 (= C517)
4xddA Apo [fefe]-hydrogenase cpi (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 3:572/582 of 4xddA
- active site: E279 (= E287), E282 (= E290), C299 (= C313), S319 (= S333), K358 (= K372), E361 (= E375), Q366 (≠ E380), C503 (= C517)
- binding fe2/s2 (inorganic) cluster: A32 (≠ T36), C34 (= C38), F35 (≠ H39), C46 (= C54), E47 (≠ R55), C49 (= C57), C62 (= C71)
- binding magnesium ion: N40 (≠ K48), D42 (≠ N50)
- binding iron/sulfur cluster: H94 (= H103), F96 (≠ N105), K97 (≠ D106), C98 (= C107), C101 (= C110), R104 (≠ C113), C107 (= C116), L110 (≠ Q119), K146 (= K154), C147 (= C155), L148 (≠ I156), L149 (≠ F157), C150 (= C158), G151 (≠ R159), C153 (= C161), C157 (= C165), T161 (≠ Q169), A165 (= A173), M166 (≠ L174), I177 (= I185), C190 (= C198), L191 (≠ T199), L192 (≠ Y200), C193 (= C201), G194 (= G202), Q195 (= Q203), C196 (= C204), C200 (= C208), P201 (= P209), V202 (= V210), A204 (= A212), L205 (= L213), C300 (= C314), C355 (= C369), M497 (= M511), A498 (= A512), C499 (= C513), C503 (= C517)
5oefA Active semisynthetic [fefe]-hydrogenase cpi with aza-diselenato- bridged [2fe] cofactor (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 3:572/574 of 5oefA
- active site: E279 (= E287), E282 (= E290), C299 (= C313), S319 (= S333), K358 (= K372), E361 (= E375), Q366 (≠ E380), C503 (= C517)
- binding dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethaneselenato- 1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+): A230 (= A238), P231 (= P239), S232 (≠ A240), C299 (= C313), P324 (= P338), Q325 (= Q339), M353 (= M367), P354 (= P368), K358 (= K372), F417 (= F431), M497 (= M511), C503 (= C517)
- binding fe2/s2 (inorganic) cluster: C34 (= C38), F35 (≠ H39), K45 (≠ S53), C46 (= C54), C49 (= C57), C62 (= C71)
- binding magnesium ion: N40 (≠ K48), D42 (≠ N50)
- binding iron/sulfur cluster: H94 (= H103), F96 (≠ N105), K97 (≠ D106), C98 (= C107), C101 (= C110), R103 (≠ K112), R104 (≠ C113), C107 (= C116), L110 (≠ Q119), C147 (= C155), L148 (≠ I156), L149 (≠ F157), C150 (= C158), G151 (≠ R159), C153 (= C161), C157 (= C165), T161 (≠ Q169), A165 (= A173), M166 (≠ L174), I177 (= I185), C190 (= C198), L191 (≠ T199), L192 (≠ Y200), C193 (= C201), G194 (= G202), C196 (= C204), C200 (= C208), P201 (= P209), V202 (= V210), A204 (= A212), L205 (= L213), C300 (= C314), C355 (= C369), M497 (= M511), A498 (= A512), C499 (= C513), C503 (= C517)
3c8yA 1.39 angstrom crystal structure of fe-only hydrogenase (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 3:572/574 of 3c8yA
- active site: E279 (= E287), E282 (= E290), C299 (= C313), S319 (= S333), K358 (= K372), E361 (= E375), Q366 (≠ E380), C503 (= C517)
- binding fe2/s2 (inorganic) cluster: A32 (≠ T36), C34 (= C38), F35 (≠ H39), K45 (≠ S53), C46 (= C54), E47 (≠ R55), C49 (= C57), C62 (= C71)
- binding 2 iron/2 sulfur/3 carbonyl/2 cyanide/water/methylether cluster: A230 (= A238), P231 (= P239), S232 (≠ A240), C299 (= C313), P324 (= P338), Q325 (= Q339), M353 (= M367), P354 (= P368), K358 (= K372), F417 (= F431), M497 (= M511), C503 (= C517)
- binding iron/sulfur cluster: H94 (= H103), F96 (≠ N105), K97 (≠ D106), C98 (= C107), C101 (= C110), R104 (≠ C113), C107 (= C116), L110 (≠ Q119), C147 (= C155), L148 (≠ I156), L149 (≠ F157), C150 (= C158), G151 (≠ R159), C153 (= C161), C157 (= C165), T161 (≠ Q169), A165 (= A173), M166 (≠ L174), I177 (= I185), C190 (= C198), L191 (≠ T199), L192 (≠ Y200), C193 (= C201), G194 (= G202), Q195 (= Q203), C196 (= C204), C200 (= C208), P201 (= P209), A203 (≠ G211), A204 (= A212), L205 (= L213), C300 (= C314), C355 (= C369), M497 (= M511), A498 (= A512), C499 (= C513), C503 (= C517)
1c4cA Binding of exogenously added carbon monoxide at the active site of the fe-only hydrogenase (cpi) from clostridium pasteurianum (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 3:572/574 of 1c4cA
- active site: E279 (= E287), E282 (= E290), C299 (= C313), S319 (= S333), K358 (= K372), E361 (= E375), Q366 (≠ E380), C503 (= C517)
- binding fe2/s2 (inorganic) cluster: A32 (≠ T36), C34 (= C38), F35 (≠ H39), K45 (≠ S53), C46 (= C54), E47 (≠ R55), C49 (= C57), C62 (= C71)
- binding 2 iron/2 sulfur/6 carbonyl/1 water inorganic cluster: A230 (= A238), P231 (= P239), S232 (≠ A240), C299 (= C313), P324 (= P338), Q325 (= Q339), M353 (= M367), P354 (= P368), K358 (= K372), F417 (= F431), M497 (= M511), C503 (= C517)
- binding iron/sulfur cluster: H94 (= H103), F96 (≠ N105), K97 (≠ D106), C98 (= C107), C101 (= C110), R104 (≠ C113), C107 (= C116), C147 (= C155), L148 (≠ I156), L149 (≠ F157), C150 (= C158), C153 (= C161), C157 (= C165), M166 (≠ L174), I177 (= I185), C190 (= C198), L191 (≠ T199), L192 (≠ Y200), C193 (= C201), G194 (= G202), C196 (= C204), C200 (= C208), P201 (= P209), V202 (= V210), A203 (≠ G211), A204 (= A212), L205 (= L213), C300 (= C314), C355 (= C369), M497 (= M511), A498 (= A512), C499 (= C513), C503 (= C517), G506 (= G520)
1c4aA Binding of exogenously added carbon monoxide at the active site of the fe-only hydrogenase (cpi) from clostridium pasteurianum (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 3:572/574 of 1c4aA
- active site: E279 (= E287), E282 (= E290), C299 (= C313), S319 (= S333), K358 (= K372), E361 (= E375), Q366 (≠ E380), C503 (= C517)
- binding fe2/s2 (inorganic) cluster: A32 (≠ T36), C34 (= C38), F35 (≠ H39), K45 (≠ S53), C46 (= C54), E47 (≠ R55), C49 (= C57), C62 (= C71)
- binding 2 iron/2 sulfur/5 carbonyl/2 water inorganic cluster: A230 (= A238), P231 (= P239), S232 (≠ A240), C299 (= C313), P324 (= P338), M353 (= M367), P354 (= P368), K358 (= K372), F417 (= F431), M497 (= M511), C503 (= C517)
- binding iron/sulfur cluster: H94 (= H103), K97 (≠ D106), C98 (= C107), C101 (= C110), R104 (≠ C113), C107 (= C116), L140 (≠ I148), K146 (= K154), C147 (= C155), L148 (≠ I156), L149 (≠ F157), C150 (= C158), G151 (≠ R159), C153 (= C161), C157 (= C165), T161 (≠ Q169), A165 (= A173), M166 (≠ L174), I177 (= I185), C190 (= C198), L191 (≠ T199), L192 (≠ Y200), C193 (= C201), G194 (= G202), C196 (= C204), C200 (= C208), P201 (= P209), V202 (= V210), A203 (≠ G211), A204 (= A212), L205 (= L213), C300 (= C314), C355 (= C369), M497 (= M511), A498 (= A512), C499 (= C513), C503 (= C517), G506 (= G520)
P29166 Iron hydrogenase 1; CpI; Fe-only hydrogenase; [Fe] hydrogenase; EC 1.12.7.2 from Clostridium pasteurianum (see 2 papers)
38% identity, 98% coverage: 7:582/588 of query aligns to 3:572/574 of P29166
- C34 (= C38) binding
- C46 (= C54) binding
- C49 (= C57) binding
- C62 (= C71) binding
- H94 (= H103) binding
- C98 (= C107) binding
- C101 (= C110) binding
- C107 (= C116) binding
- C147 (= C155) binding
- C150 (= C158) binding
- C153 (= C161) binding
- C157 (= C165) binding
- C190 (= C198) binding
- C193 (= C201) binding
- C196 (= C204) binding
- C200 (= C208) binding
- C300 (= C314) binding
- C355 (= C369) binding
- C499 (= C513) binding
- C503 (= C517) binding ; binding
5byrA Semisynthetic [fefe]-hydrogenase cpi with propane-dithiolato-bridged [2fe] cofactor (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 2:571/571 of 5byrA
- active site: E278 (= E287), E281 (= E290), C298 (= C313), S318 (= S333), K357 (= K372), E360 (= E375), Q365 (≠ E380), C502 (= C517)
- binding bis(cyanido-kappaC)(dicarbonyl)-mu-(oxomethylidene)[mu-propane-1,3-bis(thiolate)-1kappa~2~S~1~,S~3~:2kappa~2~S~1~,S~3~]diiron(2+): A229 (= A238), P230 (= P239), S231 (≠ A240), I267 (≠ T276), C298 (= C313), P323 (= P338), Q324 (= Q339), M352 (= M367), P353 (= P368), K357 (= K372), F416 (= F431), M496 (= M511), C502 (= C517)
- binding fe2/s2 (inorganic) cluster: A31 (≠ T36), C33 (= C38), F34 (≠ H39), C45 (= C54), E46 (≠ R55), C48 (= C57), C61 (= C71)
- binding magnesium ion: N39 (≠ K48), D41 (≠ N50), E281 (= E290), H564 (≠ E575), H568 (= H579)
- binding iron/sulfur cluster: H93 (= H103), F95 (≠ N105), K96 (≠ D106), C97 (= C107), C100 (= C110), R103 (≠ C113), C106 (= C116), C146 (= C155), L147 (≠ I156), L148 (≠ F157), C149 (= C158), G150 (≠ R159), C152 (= C161), C156 (= C165), A164 (= A173), M165 (≠ L174), I176 (= I185), C189 (= C198), L190 (≠ T199), L191 (≠ Y200), C192 (= C201), G193 (= G202), Q194 (= Q203), C195 (= C204), C199 (= C208), P200 (= P209), V201 (= V210), A202 (≠ G211), A203 (= A212), L204 (= L213), C299 (= C314), C354 (= C369), M496 (= M511), A497 (= A512), C498 (= C513), C502 (= C517)
4xdcA Active semisynthetic [fefe]-hydrogenase cpi with aza-dithiolato- bridged [2fe] cofactor (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 3:572/581 of 4xdcA
- active site: E279 (= E287), E282 (= E290), C299 (= C313), S319 (= S333), K358 (= K372), E361 (= E375), Q366 (≠ E380), C503 (= C517)
- binding dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+): A230 (= A238), P231 (= P239), S232 (≠ A240), C299 (= C313), P324 (= P338), Q325 (= Q339), M353 (= M367), P354 (= P368), K358 (= K372), F417 (= F431), M497 (= M511), C503 (= C517)
- binding fe2/s2 (inorganic) cluster: A32 (≠ T36), C34 (= C38), F35 (≠ H39), C46 (= C54), E47 (≠ R55), C49 (= C57), C62 (= C71)
- binding magnesium ion: N40 (≠ K48), D42 (≠ N50)
- binding iron/sulfur cluster: H94 (= H103), F96 (≠ N105), K97 (≠ D106), C98 (= C107), C101 (= C110), R104 (≠ C113), C107 (= C116), C147 (= C155), L148 (≠ I156), L149 (≠ F157), C150 (= C158), G151 (≠ R159), C153 (= C161), C157 (= C165), T161 (≠ Q169), A165 (= A173), M166 (≠ L174), I177 (= I185), C190 (= C198), L191 (≠ T199), L192 (≠ Y200), C193 (= C201), G194 (= G202), Q195 (= Q203), C196 (= C204), C200 (= C208), P201 (= P209), V202 (= V210), A203 (≠ G211), A204 (= A212), L205 (= L213), C300 (= C314), C355 (= C369), M497 (= M511), A498 (= A512), C499 (= C513), C503 (= C517)
8aioA Co-bound [fefe]-hydrogenase i from clostridium pasteurianum (cpi) (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 3:572/573 of 8aioA
- binding fe2/s2 (inorganic) cluster: A32 (≠ T36), C34 (= C38), F35 (≠ H39), C46 (= C54), E47 (≠ R55), C49 (= C57), C62 (= C71)
- binding magnesium ion: N40 (≠ K48), D42 (≠ N50)
- binding Binuclear [FeFe], di(thiomethyl)amine, carbon monoxide, cyanide cluster (-CO form): A230 (= A238), P231 (= P239), S232 (≠ A240), C299 (= C313), P324 (= P338), Q325 (= Q339), M353 (= M367), P354 (= P368), K358 (= K372), F417 (= F431), M497 (= M511), C503 (= C517)
- binding iron/sulfur cluster: H94 (= H103), F96 (≠ N105), K97 (≠ D106), C98 (= C107), C101 (= C110), C107 (= C116), K146 (= K154), C147 (= C155), L148 (≠ I156), L149 (≠ F157), C150 (= C158), G151 (≠ R159), C153 (= C161), C157 (= C165), A165 (= A173), M166 (≠ L174), I177 (= I185), C190 (= C198), L191 (≠ T199), L192 (≠ Y200), C193 (= C201), G194 (= G202), C196 (= C204), C200 (= C208), P201 (= P209), V202 (= V210), A204 (= A212), L205 (= L213), C300 (= C314), C355 (= C369), M497 (= M511), C499 (= C513), C503 (= C517)
8pvmA Formaldehyde-inhibited [fefe]-hydrogenase cpi from clostridium pasteurianum, variant c299d (see paper)
38% identity, 98% coverage: 7:582/588 of query aligns to 3:572/573 of 8pvmA
- binding dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+): A230 (= A238), P231 (= P239), S232 (≠ A240), D299 (≠ C313), P324 (= P338), Q325 (= Q339), M353 (= M367), P354 (= P368), K358 (= K372), F417 (= F431), M497 (= M511), C503 (= C517)
- binding methyl radical: N38 (≠ T45), C39 (= C46), K159 (≠ D167)
- binding fe2/s2 (inorganic) cluster: A32 (≠ T36), C34 (= C38), F35 (≠ H39), K45 (≠ S53), C46 (= C54), E47 (≠ R55), C49 (= C57), C62 (= C71)
- binding magnesium ion: N40 (≠ K48), D42 (≠ N50)
- binding iron/sulfur cluster: H94 (= H103), F96 (≠ N105), K97 (≠ D106), C98 (= C107), C101 (= C110), R103 (≠ K112), R104 (≠ C113), C107 (= C116), K146 (= K154), C147 (= C155), L148 (≠ I156), L149 (≠ F157), C150 (= C158), G151 (≠ R159), C153 (= C161), C157 (= C165), T161 (≠ Q169), A165 (= A173), M166 (≠ L174), I177 (= I185), C190 (= C198), L191 (≠ T199), L192 (≠ Y200), C193 (= C201), G194 (= G202), C196 (= C204), C200 (= C208), P201 (= P209), V202 (= V210), A204 (= A212), L205 (= L213), C300 (= C314), C355 (= C369), M497 (= M511), A498 (= A512), C499 (= C513), C503 (= C517)
7p8na Tmhydabc- t. Maritima hydrogenase with bridge closed (see paper)
39% identity, 98% coverage: 6:582/588 of query aligns to 1:548/642 of 7p8na
- binding fe2/s2 (inorganic) cluster: N32 (≠ T36), C34 (= C38), Y42 (≠ C46), G43 (≠ A52), C45 (= C54), R46 (= R55), C48 (= C57), C60 (= C71)
- binding iron/sulfur cluster: H92 (= H103), D95 (= D106), C96 (= C107), C99 (= C110), C105 (= C116), Q108 (= Q119), C143 (= C155), I144 (= I156), L145 (≠ F157), C146 (= C158), G147 (≠ R159), D148 (≠ R160), C149 (= C161), C153 (= C165), V161 (≠ A173), C186 (= C198), V187 (≠ T199), L188 (≠ Y200), C189 (= C201), G190 (= G202), C192 (= C204), C196 (= C208), P197 (= P209), T198 (≠ V210), A200 (= A212), L201 (= L213), C295 (= C314), C350 (= C369), M480 (= M511), A481 (= A512), C482 (= C513), C486 (= C517)
Sites not aligning to the query:
7qv7D Cryo-em structure of hydrogen-dependent co2 reductase. (see paper)
43% identity, 73% coverage: 151:582/588 of query aligns to 4:444/448 of 7qv7D
- binding dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+): T147 (= T276), C178 (= C313), Q204 (= Q339), M232 (= M367), K237 (= K372), C382 (= C517)
- binding iron/sulfur cluster: C10 (= C155), T11 (≠ I156), G12 (≠ F157), C13 (= C158), R14 (= R159), C16 (= C161), C20 (= C165), P21 (≠ N166), A24 (≠ Q169), I35 (≠ F181), C40 (= C198), V41 (≠ T199), C43 (= C201), G44 (= G202), C46 (= C204), C50 (= C208), C179 (= C314), C234 (= C369), C236 (≠ A371), K237 (= K372), C378 (= C513), G381 (= G516), C382 (= C517)
6ttlA Crystal structure of [fefe]-hydrogenase cba5h (partial) from clostridium beijerinckii in hinact state (see paper)
49% identity, 65% coverage: 199:583/588 of query aligns to 98:477/479 of 6ttlA
- active site: E186 (= E287), E189 (= E290), C206 (= C313), S226 (= S333), K265 (= K372), E268 (= E375), E273 (= E380), C410 (= C517)
- binding dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+): A137 (= A238), P138 (= P239), A139 (= A240), C206 (= C313), C207 (= C314), P231 (= P338), M232 (≠ Q339), M260 (= M367), P261 (= P368), K265 (= K372), F324 (= F431), V330 (= V437), M404 (= M511), C410 (= C517)
- binding iron/sulfur cluster: C207 (= C314), C262 (= C369), A405 (= A512), C406 (= C513), G409 (= G516), C410 (= C517)
6gl6A Apo [fefe]-hydrogenase hyda1 from chlamydomonas reinhardtii, variant c377h (see paper)
44% identity, 62% coverage: 218:582/588 of query aligns to 3:401/406 of 6gl6A
- active site: E77 (= E287), E80 (= E290), C100 (= C313), S120 (= S333), K159 (= K372), E162 (= E375), W167 (≠ E380), C337 (= C517)
- binding iron/sulfur cluster: C101 (= C314), C156 (= C369), R158 (≠ A371), M331 (= M511), H333 (≠ C513), C337 (= C517)
- binding sulfite ion: C156 (= C369), T157 (≠ L370), R158 (≠ A371), H333 (≠ C513), G341 (= G521)
Query Sequence
>349652 FitnessBrowser__Btheta:349652
MEEKQITLQIDGHFITVPEGSTILEAACKIGINIPTLCHIDLKGTCIKNNPASCRICVVE
VAGRRNLAPACATRCTEGMVVKTSTLRVMNARKVVAELILSDHPNDCLTCPKCGNCELQT
LALRFNIREMPFNGGELSPRKREVTSSIVRNMDKCIFCRRCESVCNDVQTVGALGAIRRG
FNTTIAPAFDRMMKDSECTYCGQCVAVCPVGALTERDYTNRLLDDLADPDKIVIVQTAPA
VRAALGEEFGLPPGTLVTGKMVYALRELGFDYVFDTDFAADLTIMEEGSEILNRLTRYLD
GDKSVRLPILTSCCPAWVNFFEHHFPDMLDIPSTARSPQQMFGSIAKSYWAEKMGIPREK
LVVVSIMPCLAKKYECDRDEFKVNGVPDVDYSISTRELARLIKRANIGFTLVLDSPFDNP
MGESTGAGVIFGTTGGVMEAALRSVYEIYTGQPLKNVNFEQVRGLSGVRRATIDLNGFEL
KVGIAHGLGNARHLLEDIRNGHNEYHVIEIMACPGGCIGGGGQPLHHGNSDVLYARANAL
YREDANKPLRKSHDNPYIQKLYEEYLGKPLGEKSEMLLHTHYFNKSID
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory