SitesBLAST
Comparing BWI76_RS24285 FitnessBrowser__Koxy:BWI76_RS24285 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
8sadA Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp/malonate complex (c2 form)
93% identity, 100% coverage: 1:395/395 of query aligns to 4:398/398 of 8sadA
- binding magnesium ion: A359 (= A356), R362 (= R359), A365 (= A362)
- binding pyridoxal-5'-phosphate: C88 (= C85), G89 (= G86), A90 (= A87), Y114 (= Y111), D188 (= D185), A210 (= A207), T212 (= T209), K213 (= K210), M222 (= M219), W343 (= W340)
8sabA Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp adduct with alanine (c2 form)
93% identity, 99% coverage: 4:395/395 of query aligns to 1:392/392 of 8sabA
- binding lysine: N9 (≠ H12), R12 (= R15), R13 (≠ S16), K14 (= K17), T17 (= T20), L330 (= L333), E341 (= E344)
- binding pyridoxal-5'-phosphate: C82 (= C85), G83 (= G86), A84 (= A87), Y108 (= Y111), D182 (= D185), A204 (= A207), T206 (= T209), K207 (= K210), M216 (= M219), W337 (= W340)
- binding alanyl-pyridoxal-5'-phosphate: C82 (= C85), G83 (= G86), A84 (= A87), Y108 (= Y111), D182 (= D185), A204 (= A207), T206 (= T209), K207 (= K210), M216 (= M219), Y335 (= Y338), S336 (= S339), W337 (= W340), R369 (= R372)
8u99A Crystal structure of cystathionine beta lyase from klebsiella aerogenes (plp-serine adduct)
93% identity, 99% coverage: 5:395/395 of query aligns to 1:391/391 of 8u99A
- binding pyridoxal-5'-phosphate: C81 (= C85), G82 (= G86), A83 (= A87), Y107 (= Y111), D181 (= D185), T205 (= T209), K206 (= K210), M215 (= M219), W336 (= W340)
- binding serine: Y107 (= Y111), K206 (= K210), Y334 (= Y338), S335 (= S339), W336 (= W340), R368 (= R372)
8u98A Crystal structure of cystathionine beta lyase from klebsiella aerogenes (plp-glycine adduct)
93% identity, 99% coverage: 5:395/395 of query aligns to 1:391/391 of 8u98A
- binding glycine: Y107 (= Y111), K206 (= K210), Y334 (= Y338), S335 (= S339), W336 (= W340), R368 (= R372)
- binding pyridoxal-5'-phosphate: Y52 (= Y56), R54 (= R58), C81 (= C85), G82 (= G86), A83 (= A87), Y107 (= Y111), D181 (= D185), A203 (= A207), T205 (= T209), K206 (= K210), M215 (= M219), W336 (= W340)
8sa9A Crystal structure of cystathionine beta lyase from klebsiella aerogenes, plp-oxamate adduct (c2 form)
93% identity, 99% coverage: 5:395/395 of query aligns to 1:391/391 of 8sa9A
- binding pyridoxal-5'-phosphate: C81 (= C85), G82 (= G86), A83 (= A87), Y107 (= Y111), D181 (= D185), A203 (= A207), T205 (= T209), K206 (= K210), M215 (= M219), W336 (= W340)
- binding [({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino](oxo)acetic acid: C81 (= C85), G82 (= G86), A83 (= A87), Y107 (= Y111), D181 (= D185), A203 (= A207), T205 (= T209), K206 (= K210), M215 (= M219), S335 (= S339), W336 (= W340), R368 (= R372)
P06721 Cystathionine beta-lyase MetC; CBL; CL; Beta-cystathionase MetC; Cysteine desulfhydrase MetC; CD; Cysteine lyase MetC; Cysteine-S-conjugate beta-lyase MetC; EC 4.4.1.13; EC 4.4.1.28 from Escherichia coli (strain K12) (see 2 papers)
85% identity, 100% coverage: 1:395/395 of query aligns to 1:395/395 of P06721
- K210 (= K210) modified: N6-(pyridoxal phosphate)lysine
1cl1B Cystathionine beta-lyase (cbl) from escherichia coli (see paper)
85% identity, 99% coverage: 4:395/395 of query aligns to 1:392/392 of 1cl1B
2gqnA Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-nitro-benzamide (see paper)
85% identity, 99% coverage: 6:395/395 of query aligns to 2:391/391 of 2gqnA
- active site: R54 (= R58), Y107 (= Y111), D181 (= D185), K206 (= K210)
- binding (5-hydroxy-6-methyl-4-((2-(2-(2-nitrobenzamido)acetyl)hydrazinyl)methyl)pyridin-3-yl)methyl dihydrogen phosphate: C81 (= C85), G82 (= G86), A83 (= A87), Y107 (= Y111), E108 (= E112), D181 (= D185), A203 (= A207), T205 (= T209), K206 (= K210), M215 (= M219), Y334 (= Y338), S335 (= S339), W336 (= W340), R368 (= R372)
2fq6A Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-trifluoromethyl-benzamide (see paper)
85% identity, 99% coverage: 6:395/395 of query aligns to 2:391/391 of 2fq6A
- active site: R54 (= R58), Y107 (= Y111), D181 (= D185), K206 (= K210)
- binding phosphoric acid mono-(5-hydroxy-6-methyl-4-{[2-(2-trifluoromethyl-benzoylamino)-acetyl]-hydrazonomethyl}-pyridin-3-ylmethyl)ester: C81 (= C85), G82 (= G86), A83 (= A87), Y107 (= Y111), P109 (= P113), D181 (= D185), A203 (= A207), T205 (= T209), K206 (= K210), M215 (= M219), Y334 (= Y338), S335 (= S339), W336 (= W340), R368 (= R372)
1cl2A Cystathionine beta-lyase (cbl) from escherichia coli in complex with aminoethoxyvinylglycine (see paper)
85% identity, 99% coverage: 6:395/395 of query aligns to 2:391/391 of 1cl2A
- active site: R54 (= R58), Y107 (= Y111), D181 (= D185), K206 (= K210)
- binding (2E,3E)-4-(2-aminoethoxy)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: C81 (= C85), G82 (= G86), A83 (= A87), Y107 (= Y111), D181 (= D185), A203 (= A207), T205 (= T209), K206 (= K210), M215 (= M219), Y334 (= Y338), S335 (= S339), W336 (= W340), R368 (= R372)
4itxA P113s mutant of e. Coli cystathionine beta-lyase metc inhibited by reaction with l-ala-p (see paper)
85% identity, 99% coverage: 6:395/395 of query aligns to 2:391/391 of 4itxA
- active site: R54 (= R58), Y107 (= Y111), D181 (= D185), K206 (= K210)
- binding {1-[(3-hydroxy-methyl-5-phosphonooxy-methyl-pyridin-4-ylmethyl)-amino]-ethyl}-phosphonic acid: C81 (= C85), G82 (= G86), A83 (= A87), Y107 (= Y111), D181 (= D185), A203 (= A207), T205 (= T209), K206 (= K210), M215 (= M219), Y334 (= Y338), S335 (= S339), W336 (= W340), R368 (= R372)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
30% identity, 98% coverage: 6:394/395 of query aligns to 3:373/373 of 4l0oH
- active site: R40 (= R58), Y92 (= Y111), D164 (= D185), K189 (= K210)
- binding pyridoxal-5'-phosphate: Y38 (= Y56), R40 (= R58), S67 (≠ C85), G68 (= G86), L69 (≠ A87), Y92 (= Y111), D164 (= D185), S186 (≠ A207), T188 (= T209), K189 (= K210)
7d7oB Crystal structure of cystathionine gamma-lyase from bacillus cereus atcc 14579 (see paper)
31% identity, 97% coverage: 8:392/395 of query aligns to 5:377/377 of 7d7oB
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
27% identity, 97% coverage: 8:391/395 of query aligns to 7:389/393 of 1e5fA
- active site: R55 (= R58), Y108 (= Y111), D181 (= D185), K206 (= K210)
- binding pyridoxal-5'-phosphate: Y53 (= Y56), R55 (= R58), G83 (= G86), M84 (≠ A87), Y108 (= Y111), D181 (= D185), S203 (≠ A207), K206 (= K210)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
27% identity, 97% coverage: 8:391/395 of query aligns to 7:389/394 of 1e5eA
- active site: R55 (= R58), Y108 (= Y111), D181 (= D185), K206 (= K210)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y56), R55 (= R58), G83 (= G86), M84 (≠ A87), Y108 (= Y111), N155 (≠ S158), D181 (= D185), S203 (≠ A207), T205 (= T209), K206 (= K210), S335 (= S339), T350 (≠ A356), R370 (= R372)
3aeoA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine alpha, beta-enamine-pyridoxamine- 5'-phosphate
29% identity, 91% coverage: 28:387/395 of query aligns to 24:380/387 of 3aeoA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y51 (= Y56), R53 (= R58), G81 (= G86), M82 (≠ A87), Y106 (= Y111), E149 (= E154), N153 (≠ S158), D178 (= D185), S200 (≠ A207), S202 (≠ T209), K203 (= K210), V329 (≠ Y338), S330 (= S339), T345 (vs. gap), R365 (= R372)
3aelA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine imine-pyridoxamine-5'-phosphate and alpha-amino-alpha, beta-butenoic acid-pyridoxal-5'-phosphate
29% identity, 91% coverage: 28:387/395 of query aligns to 24:380/387 of 3aelA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]-4-(methylsulfanyl)butanoic acid: Y51 (= Y56), R53 (= R58)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: G81 (= G86), M82 (≠ A87), Y106 (= Y111), E149 (= E154), N153 (≠ S158), D178 (= D185), T180 (= T187), S200 (≠ A207), S202 (≠ T209), K203 (= K210), S330 (= S339), T345 (vs. gap), R365 (= R372)
3aejC Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 tetramer containing michaelis complex and methionine- pyridoxal-5'-phosphate
29% identity, 91% coverage: 28:387/395 of query aligns to 24:380/387 of 3aejC
- active site: R53 (= R58), Y106 (= Y111), D178 (= D185), K203 (= K210)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: F42 (≠ T46), Y51 (= Y56), R53 (= R58)
- binding methionine: Y106 (= Y111), K203 (= K210), S330 (= S339), L331 (≠ W340), T345 (vs. gap), R365 (= R372)
3aejA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 tetramer containing michaelis complex and methionine- pyridoxal-5'-phosphate
29% identity, 91% coverage: 28:387/395 of query aligns to 24:380/387 of 3aejA
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: Y51 (= Y56), R53 (= R58), G81 (= G86), M82 (≠ A87), Y106 (= Y111), E149 (= E154), N153 (≠ S158), D178 (= D185), S200 (≠ A207), S202 (≠ T209), K203 (= K210), S330 (= S339), L331 (≠ W340), T345 (vs. gap), R365 (= R372)
8j6nA Crystal structure of cystathionine gamma-lyase in complex with compound 1 (see paper)
29% identity, 97% coverage: 4:387/395 of query aligns to 7:381/390 of 8j6nA
- binding [6-methyl-4-[(~{E})-(oxamoylhydrazinylidene)methyl]-5-oxidanyl-pyridin-3-yl]methyl dihydrogen phosphate: Y51 (= Y56), R53 (= R58), G81 (= G86), L82 (≠ A87), Y105 (= Y111), E148 (= E154), N152 (≠ S158), D178 (= D185), S200 (≠ A207), T202 (= T209), K203 (= K210), E330 (≠ Y338), S331 (= S339), T346 (≠ E353), R366 (= R372)
Query Sequence
>BWI76_RS24285 FitnessBrowser__Koxy:BWI76_RS24285
MADKHLDTALVHAGRSKKYTQGSVNSVIQRASSLVFDTVEAKKHATRNRAKGELFYGRRG
TLTHFSLQEAMCELEGGAGCALFPCGAAAVANTILAFVEQGDHILVTNTAYEPTQDFCTK
ILAKLGVTTGWFDPLIGGDIARLVQPNTRVVFLESPGSITMEVHDVPAIVAAVRRVAPEA
IIMIDNTWAAGVLFKALEFGIDISIQAGTKYLIGHSDAMVGTAVSNERCWAQLRENAYLM
GQMVDADTAYMTSRGLRTLAVRLRQHHESSLQIAEWLAQHPQVARVNHPALPGSKGHEFW
QRDFTGSSGLFSFVLNKRLTDAELSAYLDHFSLFSMAYSWGGFESLILANQPEHIAAIRP
DAEVDFSGTLIRLHIGLENVTDLQDDLAAGFARIV
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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