SitesBLAST
Comparing AZOBR_RS14960 FitnessBrowser__azobra:AZOBR_RS14960 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)
6tg9A Cryo-em structure of nadh reduced form of NAD+-dependent formate dehydrogenase from rhodobacter capsulatus (see paper)
68% identity, 98% coverage: 7:926/938 of query aligns to 8:935/949 of 6tg9A
- active site: K289 (= K280), C380 (= C371), H381 (= H372), L545 (= L536), G582 (= G573), Q583 (= Q574)
- binding fe2/s2 (inorganic) cluster: C51 (= C51), V59 (≠ Y59), G60 (= G60), C62 (= C62), C65 (= C65), C79 (= C79)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: C255 (= C246), K289 (= K280), R351 (= R342), C352 (= C343), C380 (= C371), G414 (= G405), A415 (= A406), D419 (= D410), G420 (= G411), H421 (= H412), P443 (= P434), R444 (= R435), P464 (= P455), N467 (= N458), L545 (= L536), G546 (= G537), H550 (= H541), G582 (= G573), Q583 (= Q574), Q583 (= Q574), G649 (= G640), E650 (= E641), S655 (= S646), N680 (= N671), S693 (≠ T684), K698 (= K689), D724 (≠ E715), T820 (= T811), T821 (= T812), R823 (= R814), R823 (= R814), I824 (= I815), L825 (= L816), N829 (= N820), V830 (= V821), Q833 (= Q824), N902 (= N893), Y918 (= Y909), K919 (= K910)
- binding iron/sulfur cluster: H111 (= H111), C115 (= C115), C118 (= C118), A120 (≠ T120), C124 (= C124), C176 (= C166), I177 (= I167), V178 (= V168), C179 (= C169), M180 (≠ S170), C182 (= C172), C186 (= C176), I206 (≠ V196), C218 (= C209), S220 (= S211), C221 (= C212), G222 (= G213), C224 (= C215), C228 (= C219), T230 (= T221), A231 (= A222), C252 (= C243), Y254 (= Y245), C255 (= C246), V257 (= V248), C259 (= C250), F261 (= F252), C287 (= C278), K289 (= K280), V423 (= V414)
7vw6A Cryo-em structure of formate dehydrogenase 1 from methylorubrum extorquens am1 (see paper)
36% identity, 96% coverage: 19:917/938 of query aligns to 2:911/913 of 7vw6A
- binding fe2/s2 (inorganic) cluster: H32 (≠ K49), C34 (= C51), H35 (vs. gap), G45 (= G60), C47 (= C62), R48 (= R63), C50 (= C65), C64 (= C79)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: K263 (= K280), K339 (≠ R342), C364 (= C367), C368 (= C371), G402 (= G405), N404 (= N407), N408 (≠ G411), D431 (= D433), P432 (= P434), R433 (= R435), F447 (≠ L453), G450 (= G456), D452 (≠ N458), G525 (= G535), M526 (≠ L536), G527 (= G537), Q530 (≠ E540), H531 (= H541), G563 (= G573), Q564 (= Q574), G630 (= G640), N632 (≠ D642), S636 (= S646), Q656 (= Q666), D657 (= D667), L658 (= L668), T805 (= T812), R807 (= R814), R807 (= R814), V808 (≠ I815), L809 (= L816), H811 (= H818), W812 (≠ Y819), H813 (≠ N820), H813 (≠ N820), T814 (≠ V821), M817 (≠ Q824), F879 (= F885), N887 (= N893), F903 (≠ Y909), K904 (= K910)
- binding iron/sulfur cluster: C145 (= C166), I146 (= I167), Q147 (≠ V168), C148 (= C169), N149 (≠ S170), C151 (= C172), C155 (= C176), N161 (≠ T182), V163 (≠ A184), I164 (≠ L185), V175 (= V196), C188 (= C209), V189 (= V210), A190 (≠ S211), C191 (= C212), G192 (= G213), C194 (= C215), C198 (= C219), P199 (= P220), T200 (= T221), A202 (≠ T223), L203 (= L224), C227 (= C243), C230 (= C246), C234 (= C250), C261 (= C278), K263 (= K280), G264 (= G281), V411 (= V414)
1fdiA Oxidized form of formate dehydrogenase h from e. Coli complexed with the inhibitor nitrite (see paper)
38% identity, 72% coverage: 238:916/938 of query aligns to 3:685/715 of 1fdiA
- active site: C11 (= C246), L41 (≠ S277), C42 (= C278), K44 (= K280), S108 (= S340), R110 (= R342), D134 (= D365), C140 (= C371), H141 (= H372), S180 (≠ G411), M297 (≠ L536), R333 (= R572), G334 (= G573), Q335 (= Q574)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: K44 (= K280), R110 (= R342), G111 (≠ C343), V139 (= V370), C140 (= C371), F173 (≠ I404), G174 (= G405), Y175 (≠ A406), N176 (= N407), D179 (= D410), S180 (≠ G411), C201 (≠ I432), D202 (= D433), P203 (= P434), R204 (= R435), L218 (= L453), G221 (= G456), N223 (= N458), G296 (= G535), M297 (≠ L536), G298 (= G537), F302 (≠ H541), G334 (= G573), Q335 (= Q574), Q335 (= Q574), G402 (= G640), E403 (= E641), T408 (≠ S646), Q428 (= Q666), D429 (= D667), I430 (≠ L668), S445 (≠ G683), D478 (≠ E715), T579 (= T812), V580 (≠ G813), R581 (= R814), R581 (= R814), E582 (≠ I815), H585 (= H818), Y586 (= Y819), S587 (≠ N820), C588 (≠ V821), Y654 (≠ F885), N662 (= N893), Y678 (= Y909), K679 (= K910)
- binding nitrite ion: C140 (= C371), H141 (= H372), R333 (= R572), G334 (= G573), V338 (= V577)
- binding iron/sulfur cluster: C8 (= C243), Y10 (= Y245), C11 (= C246), S13 (≠ V248), C15 (= C250), L41 (≠ S277), C42 (= C278), K44 (= K280), P182 (= P413), I183 (≠ V414)
P07658 Formate dehydrogenase H; Formate dehydrogenase-H subunit alpha; FDH-H; Formate-hydrogen-lyase-linked, selenocysteine-containing polypeptide; EC 1.17.98.4 from Escherichia coli (strain K12) (see 2 papers)
38% identity, 72% coverage: 238:916/938 of query aligns to 3:685/715 of P07658
- C8 (= C243) binding
- Y10 (= Y245) binding
- C11 (= C246) binding
- C15 (= C250) binding
- C42 (= C278) binding
- K44 (= K280) binding
- U140 (≠ C371) modified: nonstandard, Selenocysteine
- M297 (≠ L536) binding
- Q301 (≠ E540) binding
- Q335 (= Q574) binding
- S445 (≠ G683) binding
- D478 (≠ E715) binding
- C588 (≠ V821) binding
- Y654 (≠ F885) binding
- Q655 (≠ H886) binding
- Y678 (= Y909) binding
- K679 (= K910) binding
2iv2X Reinterpretation of reduced form of formate dehydrogenase h from e. Coli (see paper)
38% identity, 72% coverage: 238:916/938 of query aligns to 3:667/697 of 2iv2X
- active site: C11 (= C246), L41 (≠ S277), C42 (= C278), K44 (= K280), S108 (= S340), C140 (= C371), H141 (= H372), S180 (≠ G411), M297 (≠ L536), R333 (= R572), G334 (= G573), Q335 (= Q574)
- binding guanylate-o'-phosphoric acidmono-(2-amino-5,6-dimercapto-4-oxo-3,5,6,7,8a,9,10,10a-octahydro-4h-8-oxa-1,3,9,10-tetraaza-anthracen-7-ylmethyl) ester: R110 (= R342), G111 (≠ C343), T112 (= T344), A137 (= A368), Q335 (= Q574), G402 (= G640), E403 (= E641), D404 (= D642), T408 (≠ S646), A410 (≠ P648), Q428 (= Q666), D429 (= D667), I430 (≠ L668), S445 (≠ G683), D478 (≠ E715), C588 (≠ V821), Y660 (= Y909)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: K44 (= K280), F173 (≠ I404), G174 (= G405), Y175 (≠ A406), N176 (= N407), D179 (= D410), S180 (≠ G411), D202 (= D433), P203 (= P434), R204 (= R435), N223 (= N458), G296 (= G535), M297 (≠ L536), F302 (≠ H541), G334 (= G573), R581 (= R814), E582 (≠ I815), V583 (≠ L816), H585 (= H818), Y586 (= Y819), S587 (≠ N820), K661 (= K910)
- binding iron/sulfur cluster: C8 (= C243), C11 (= C246), S13 (≠ V248), C15 (= C250), L41 (≠ S277), C42 (= C278), K44 (= K280), G45 (= G281), I183 (≠ V414)
7qv7S Cryo-em structure of hydrogen-dependent co2 reductase. (see paper)
37% identity, 62% coverage: 236:813/938 of query aligns to 1:571/571 of 7qv7S
7bkbD Formate dehydrogenase - heterodisulfide reductase - formylmethanofuran dehydrogenase complex from methanospirillum hungatei (hexameric, composite structure) (see paper)
36% identity, 60% coverage: 239:797/938 of query aligns to 7:548/549 of 7bkbD
2jirA A new catalytic mechanism of periplasmic nitrate reductase from desulfovibrio desulfuricans atcc 27774 from crystallographic and epr data and based on detailed analysis of the sixth ligand (see paper)
29% identity, 73% coverage: 234:916/938 of query aligns to 1:717/720 of 2jirA
- active site: K46 (= K280), S106 (= S340), C137 (= C371), M138 (≠ H372), A177 (≠ G411), M305 (≠ L536), T341 (≠ R572), G342 (= G573), Q343 (= Q574)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: R11 (≠ A244), K46 (= K280), Q108 (≠ R342), C137 (= C371), G171 (= G405), S172 (≠ A406), N173 (= N407), E176 (≠ D410), A177 (≠ G411), D201 (= D433), P202 (= P434), R203 (= R435), F217 (≠ L453), D222 (≠ N458), C304 (≠ G535), M305 (≠ L536), G306 (= G537), Q309 (≠ E540), R310 (≠ H541), G342 (= G573), Q343 (= Q574), Q343 (= Q574), E413 (≠ G640), T414 (≠ E641), N415 (≠ D642), T419 (≠ S646), I440 (≠ V665), E441 (≠ Q666), A442 (≠ D667), P458 (≠ G683), F460 (≠ S685), S612 (≠ T812), M613 (≠ G813), R614 (= R814), R614 (= R814), I616 (≠ L816), H618 (= H818), W619 (≠ Y819), H620 (≠ N820), H620 (≠ N820), T621 (≠ V821), T623 (≠ A823), F686 (= F885), N694 (= N893), Y710 (= Y909), K711 (= K910)
- binding nitrite ion: V615 (≠ I815), F686 (= F885)
- binding iron/sulfur cluster: C10 (= C243), C13 (= C246), T15 (≠ V248), C17 (= C250), L43 (≠ S277), C44 (= C278), P179 (= P413), V180 (= V414)
2v45A A new catalytic mechanism of periplasmic nitrate reductase from desulfovibrio desulfuricans atcc 27774 from crystallographic and epr data and based on detailed analysis of the sixth ligand (see paper)
29% identity, 73% coverage: 234:916/938 of query aligns to 4:720/723 of 2v45A
- active site: K49 (= K280), S109 (= S340), C140 (= C371), M141 (≠ H372), A180 (≠ G411), M308 (≠ L536), T344 (≠ R572), G345 (= G573), Q346 (= Q574)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: R14 (≠ A244), K49 (= K280), Q111 (≠ R342), C140 (= C371), G174 (= G405), N176 (= N407), E179 (≠ D410), A180 (≠ G411), D204 (= D433), P205 (= P434), R206 (= R435), P222 (= P455), D225 (≠ N458), C307 (≠ G535), M308 (≠ L536), G309 (= G537), Q312 (≠ E540), R313 (≠ H541), G345 (= G573), Q346 (= Q574), Q346 (= Q574), E416 (≠ G640), T417 (≠ E641), N418 (≠ D642), T422 (≠ S646), I443 (≠ V665), E444 (≠ Q666), A445 (≠ D667), F446 (≠ L668), P461 (≠ G683), F463 (≠ S685), S615 (≠ T812), M616 (≠ G813), R617 (= R814), R617 (= R814), V618 (≠ I815), I619 (≠ L816), H621 (= H818), W622 (≠ Y819), H623 (≠ N820), H623 (≠ N820), T624 (≠ V821), T626 (≠ A823), F689 (= F885), N697 (= N893), Y713 (= Y909), K714 (= K910)
- binding iron/sulfur cluster: C13 (= C243), C16 (= C246), T18 (≠ V248), C20 (= C250), L46 (≠ S277), C47 (= C278), V183 (= V414)
2jiqA A new catalytic mechanism of periplasmic nitrate reductase from desulfovibrio desulfuricans atcc 27774 from crystallographic and epr data and based on detailed analysis of the sixth ligand (see paper)
29% identity, 73% coverage: 234:916/938 of query aligns to 1:717/720 of 2jiqA
- active site: K46 (= K280), S106 (= S340), C137 (= C371), M138 (≠ H372), A177 (≠ G411), M305 (≠ L536), T341 (≠ R572), G342 (= G573), Q343 (= Q574)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: R11 (≠ A244), Q108 (≠ R342), C137 (= C371), G171 (= G405), S172 (≠ A406), E176 (≠ D410), A177 (≠ G411), D201 (= D433), P202 (= P434), R203 (= R435), P219 (= P455), D222 (≠ N458), C304 (≠ G535), M305 (≠ L536), G306 (= G537), Q309 (≠ E540), R310 (≠ H541), G342 (= G573), Q343 (= Q574), Q343 (= Q574), E413 (≠ G640), T414 (≠ E641), N415 (≠ D642), T419 (≠ S646), I440 (≠ V665), E441 (≠ Q666), F443 (≠ L668), P458 (≠ G683), F460 (≠ S685), S612 (≠ T812), M613 (≠ G813), R614 (= R814), R614 (= R814), I616 (≠ L816), H618 (= H818), W619 (≠ Y819), H620 (≠ N820), H620 (≠ N820), T621 (≠ V821), T623 (≠ A823), F686 (= F885), N694 (= N893), Y710 (= Y909), K711 (= K910)
- binding nitrate ion: M251 (≠ V480), K583 (≠ R785), V589 (≠ M791), W591 (≠ T793), R593 (≠ V796), V704 (≠ A903)
- binding iron/sulfur cluster: C10 (= C243), C13 (= C246), T15 (≠ V248), C17 (= C250), L43 (≠ S277), C44 (= C278), V180 (= V414)
P81186 Periplasmic nitrate reductase; EC 1.9.6.1 from Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB) (see 3 papers)
29% identity, 73% coverage: 234:916/938 of query aligns to 36:752/755 of P81186
Sites not aligning to the query:
- 1:32 signal peptide, Tat-type signal
7t30A Structure of electron bifurcating ni-fe hydrogenase complex hydabcsl in fmn/NAD(h) bound state (see paper)
27% identity, 76% coverage: 19:730/938 of query aligns to 4:640/666 of 7t30A
- binding fe2/s2 (inorganic) cluster: C36 (= C51), G45 (= G60), C47 (= C62), R48 (= R63), C50 (= C65), C64 (= C79)
- binding iron/sulfur cluster: F93 (≠ I108), H98 (≠ L113), F99 (≠ D114), C100 (= C115), C103 (= C118), Q105 (≠ T120), C109 (= C124), L141 (≠ F159), R147 (≠ K165), C148 (= C166), L150 (≠ V168), C151 (= C169), Q152 (≠ S170), C154 (= C172), C158 (= C176), C192 (= C209), V193 (= V210), N194 (≠ S211), C195 (= C212), G196 (= G213), A197 (= A214), C198 (= C215), C202 (= C219), P203 (= P220), T204 (= T221), G205 (≠ A222), T206 (= T223), I207 (≠ L224), C229 (= C243), C232 (= C246), G235 (= G249), C236 (= C250), L263 (≠ S277), C264 (= C278), V396 (= V414)
8oh5C Cryo-em structure of the electron bifurcating transhydrogenase stnabc complex from sporomusa ovata (state 2) (see paper)
29% identity, 67% coverage: 154:783/938 of query aligns to 601:1134/1172 of 8oh5C
- binding iron/sulfur cluster: C613 (= C166), V614 (≠ I167), L615 (≠ V168), C616 (= C169), G617 (≠ S170), C619 (= C172), C623 (= C176), I643 (≠ V196), C656 (= C209), I657 (≠ V210), S658 (= S211), C659 (= C212), G660 (= G213), C662 (= C215), C666 (= C219), G669 (≠ A222), A670 (≠ T223), C692 (= C243), Y694 (= Y245), C695 (= C246), C699 (= C250), C725 (= C278), R727 (≠ K280), G728 (= G281), V853 (= V414)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 199, 201, 202, 203, 222, 223, 229, 230, 235, 239, 264, 265, 285, 288, 332, 471, 477, 479
- binding fe2/s2 (inorganic) cluster: 36, 45, 47, 48, 50, 64
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 330, 331, 332, 333, 353, 354, 355, 432, 433, 434, 477
- binding iron/sulfur cluster: 96, 98, 100, 102, 104, 108, 147, 149, 151, 155, 156, 164, 170, 480, 562, 563, 565, 567, 573
2nyaA Crystal structure of the periplasmic nitrate reductase (nap) from escherichia coli (see paper)
24% identity, 72% coverage: 243:916/938 of query aligns to 10:789/791 of 2nyaA
- active site: N44 (≠ S277), C45 (= C278), K47 (= K280), C143 (= C371), M144 (≠ H372), M183 (≠ G411), M336 (≠ L536), T372 (≠ R572), G373 (= G573), Q374 (= Q574)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: R11 (≠ A244), K47 (= K280), Q114 (≠ R342), N139 (≠ C367), C143 (= C371), W176 (≠ I404), G177 (= G405), M183 (≠ G411), S207 (≠ I430), T208 (≠ V431), Y209 (≠ I432), F223 (≠ L453), D228 (≠ N458), T335 (≠ G535), M336 (≠ L536), M336 (≠ L536), G337 (= G537), F338 (≠ V538), Q340 (≠ E540), G373 (= G573), Q374 (= Q574), Q374 (= Q574), C444 (≠ G640), T445 (≠ E641), N446 (≠ D642), A450 (≠ S646), S472 (≠ Q666), D473 (= D667), P474 (≠ L668), T489 (≠ G683), A490 (≠ T684), M491 (≠ S685), K495 (= K689), D522 (vs. gap), T682 (= T812), G683 (= G813), R684 (= R814), R684 (= R814), L686 (= L816), H688 (= H818), W689 (≠ Y819), H690 (≠ N820), H690 (≠ N820), T691 (≠ V821), S693 (≠ A823), F758 (= F885), N766 (= N893), F782 (≠ Y909), K783 (= K910), K784 (≠ V911)
- binding iron/sulfur cluster: C10 (= C243), C13 (= C246), C17 (= C250), C45 (= C278), I186 (≠ V414)
P33937 Periplasmic nitrate reductase; EC 1.9.6.1 from Escherichia coli (strain K12) (see 3 papers)
24% identity, 72% coverage: 243:916/938 of query aligns to 46:825/828 of P33937
- C46 (= C243) binding
- C49 (= C246) binding
- C53 (= C250) binding
- C81 (= C278) binding
- K83 (= K280) binding
- Q150 (≠ R342) binding
- N175 (≠ C367) binding
- C179 (= C371) binding
- 212:219 (vs. 404:411, 38% identical) binding
- STYQH 243:247 (≠ IVIDP 430:434) binding
- QSD 262:264 (≠ GTN 456:458) binding
- M372 (≠ L536) binding
- Q376 (≠ E540) binding
- N482 (≠ D642) binding
- SD 508:509 (≠ QD 666:667) binding
- K531 (= K689) binding
- D558 (vs. gap) binding
- 718:727 (vs. 812:821, 50% identical) binding
- N802 (= N893) binding
- K819 (= K910) binding
Sites not aligning to the query:
- 1:36 signal peptide, Tat-type signal
- 6 R→Q: Impairs interaction with NapD. Lack of nitrate reductase activity. Tat transport is blocked.
- 10 K→Q: Impairs interaction with NapD. Slight decrease in nitrate reductase activity. Minor defect in Tat transport.
- 17 A→L: Impairs interaction with NapD.; A→Q: Impairs interaction with NapD. Decrease in nitrate reductase activity. Defect in Tat transport.
8e9hG Mycobacterial respiratory complex i, fully-inserted quinone (see paper)
32% identity, 44% coverage: 18:434/938 of query aligns to 4:413/782 of 8e9hG
- binding fe2/s2 (inorganic) cluster: R35 (≠ K49), C37 (= C51), D38 (≠ A52), G46 (= G60), C48 (= C62), R49 (= R63), C51 (= C65), A63 (= A77), C65 (= C79)
- binding guanosine-5'-triphosphate: R320 (= R342)
- binding iron/sulfur cluster: H99 (= H111), D102 (= D114), C103 (= C115), C106 (= C118), G109 (≠ N121), C112 (= C124), Q115 (= Q127), C152 (= C166), V153 (≠ I167), L154 (≠ V168), C155 (= C169), A156 (≠ S170), R157 (= R171), C158 (= C172), C202 (= C219), P203 (= P220), V204 (≠ T221), A206 (≠ T223), L207 (= L224), C228 (= C243), C231 (= C246), S233 (≠ V248), C235 (= C250), N262 (≠ S277), C263 (= C278), G266 (= G281), P391 (= P413), I392 (≠ V414)
Sites not aligning to the query:
- binding guanosine-5'-triphosphate: 486, 487, 554, 556, 559, 579, 580, 582, 627, 689, 695, 696, 697
7b0nG 3.7-angstrom structure of Yarrowia lipolytica complex I with an R121M mutation in NUCM. (see paper)
31% identity, 44% coverage: 19:434/938 of query aligns to 3:410/694 of 7b0nG
- binding fe2/s2 (inorganic) cluster: C35 (= C51), G44 (= G60), C46 (= C62), R47 (= R63), C49 (= C65), C63 (= C79)
- binding iron/sulfur cluster: H95 (= H111), C99 (= C115), C102 (= C118), C108 (= C124), Q111 (= Q127), C149 (= C166), H151 (≠ V168), C152 (= C169), T153 (≠ S170), C155 (= C172), C199 (= C219), V201 (≠ T221)
7arcG Cryo-em structure of polytomella complex-i (peripheral arm) (see paper)
30% identity, 47% coverage: 23:466/938 of query aligns to 10:426/682 of 7arcG
- binding fe2/s2 (inorganic) cluster: R36 (≠ K49), C38 (= C51), Y39 (≠ A52), G47 (= G60), C49 (= C62), R50 (= R63), C52 (= C65), C66 (= C79)
- binding iron/sulfur cluster: H98 (= H111), D101 (= D114), C102 (= C115), C105 (= C118), Q107 (≠ T120), C111 (= C124), Q114 (= Q127), C150 (= C166), I151 (= I167), C153 (= C169), C156 (= C172), C200 (= C219), V202 (≠ T221), A204 (≠ T223), L205 (= L224)
- binding : K272 (≠ H290), Q274 (≠ D292), R275 (= R293), N277 (≠ T295)
Sites not aligning to the query:
8a6tA Cryo-em structure of the electron bifurcating fe-fe hydrogenase hydabc complex from thermoanaerobacter kivui in the reduced state (see paper)
42% identity, 23% coverage: 17:231/938 of query aligns to 2:211/571 of 8a6tA
- binding fe2/s2 (inorganic) cluster: C36 (= C51), D37 (≠ A52), C47 (= C62), R48 (= R63), C50 (= C65), C63 (= C79)
- binding iron/sulfur cluster: H95 (= H111), C99 (= C115), C102 (= C118), C108 (= C124), C146 (= C166), C149 (= C169), G150 (≠ S170), K151 (≠ R171), C152 (= C172), C156 (= C176), C189 (= C209), C192 (= C212), C195 (= C215), C199 (= C219), G202 (≠ A222)
Sites not aligning to the query:
- binding 2 iron/2 sulfur/5 carbonyl/2 water inorganic cluster: 229, 230, 231, 298, 323, 352, 353, 357, 412, 500
- binding iron/sulfur cluster: 299, 354, 496, 500
Q53176 Periplasmic nitrate reductase; EC 1.9.6.1 from Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides) (see paper)
24% identity, 72% coverage: 243:916/938 of query aligns to 48:828/831 of Q53176
- C48 (= C243) binding
- C51 (= C246) binding
- C55 (= C250) binding
- C83 (= C278) binding
- K85 (= K280) binding
- Q152 (≠ R342) binding
- N177 (≠ C367) binding
- C181 (= C371) binding
- 214:221 (vs. 404:411, 25% identical) binding
- GTD 264:266 (≠ GTN 456:458) binding
- M375 (≠ L536) binding
- Q379 (≠ E540) binding
- N485 (≠ D642) binding
- SD 511:512 (≠ QD 666:667) binding
- K534 (= K689) binding
- D561 (vs. gap) binding
- 721:730 (vs. 812:821, 50% identical) binding
- N805 (= N893) binding
- K822 (= K910) binding
Query Sequence
>AZOBR_RS14960 FitnessBrowser__azobra:AZOBR_RS14960
MSIQEIDYGTPARESATMVTLDIDGRTVTVPEGTSVMRAAMEAGITVPKLCATDMLDAYG
SCRLCMVEIEGRRGTPASCTTPVAPGMKVHTQNERLGRLRRGVMELYISDHPLDCLTCPT
NGNCELQDMAGAVGLRNVRYGYEGENHRAAVKDESNPYFTFDPSKCIVCSRCVRACGEVQ
GTFALTIDGRGFDSKVSPGALEQFMDSECVSCGACVQACPTATLTEKSLIELGQPEHSVI
TTCAYCGVGCSFKAEMKGTTVVRMVPHKDGGANEGHSCVKGRFAWGYATHADRQTQPMVR
ESIDDPWRVVSWEEAITYAATRLRAVQQKYGRGSIGGITSSRCTNEEVYVVQKMIRAAFG
NNNVDTCARVCHSPTGYGLKQTFGTSAGTQDFKSVDKSDVILVIGANPTDGHPVFGSRMK
KRLRQGAKLIVIDPRRIDLVRSPHVSATHHLQLRPGTNVAAMNALAHVIVTEELVDRNFV
ADRCDPMEFARWEAFVRDPRHSPENTEQYTGIPAAEMRAAARLYATGGNAAIYYGLGVTE
HSQGSTAVMGMANLAMATGNIGRDGVGVNPLRGQNNVQGSCDMGSFPHELTGYRHVSDDV
VRQQFEEVWNAALDPEPGLRIPNMFDSAVDGTFMGLFVQGEDIAQSDPNTQHVFAALRAM
EIVVVQDLFLNETAAFAHVFLPGTSFLEKDGTFTNAERRINRVRPVMPSKTGKQEWEVVC
DLATAMGYPMFYRSGAQIMDEIARLTPTFSGVSFEKLDRVGSVQWPCTDEDSVGTPIMHA
DGFVRGQGRFMITEYVPTEERASRFYPLILTTGRILSHYNVGAQTRRTANVAWHPEDILE
VHAHDAEERGIRDGDLVSIASRIGATTLRARISDRMPQGVVYTTFHHPVTGANVVTTENS
DWATNCPEYKVTAVQVTLSNHPSDWQIRRGDLVEVAAE
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