SitesBLAST
Comparing HSERO_RS17625 FitnessBrowser__HerbieS:HSERO_RS17625 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)
P46883 Primary amine oxidase; 2-phenylethylamine oxidase; Copper amine oxidase; Tyramine oxidase; EC 1.4.3.21 from Escherichia coli (strain K12) (see 6 papers)
68% identity, 100% coverage: 3:747/748 of query aligns to 12:755/757 of P46883
- 411:422 (vs. 403:414, 92% identical) binding
- D413 (= D405) active site, Proton acceptor
- VGNYDY 493:498 (= VGNYDY 485:490) binding
- Y496 (= Y488) active site, Schiff-base intermediate with substrate; via topaquinone; modified: 2',4',5'-topaquinone
- H554 (= H546) binding
- H556 (= H548) binding
- D563 (= D555) binding
- L564 (= L556) binding
- D565 (= D557) binding
- E603 (= E595) binding
- Y697 (≠ F689) binding
- D700 (= D692) binding
- E702 (≠ Q694) binding
- D708 (= D700) binding
- A709 (≠ D701) binding
- H719 (= H711) binding
Sites not aligning to the query:
1oacB Crystal structure of a quinoenzyme: copper amine oxidase of escherichia coli at 2 angstroems resolution (see paper)
70% identity, 97% coverage: 26:747/748 of query aligns to 1:721/723 of 1oacB
- active site: Y365 (= Y391), D379 (= D405), Y462 (= Y488), H520 (= H546), H522 (= H548), H685 (= H711)
- binding calcium ion: D529 (= D555), L530 (= L556), D531 (= D557), E569 (= E595), Y663 (≠ F689), D666 (= D692), E668 (≠ Q694), D674 (= D700), A675 (≠ D701)
- binding copper (ii) ion: Y462 (= Y488), H520 (= H546), H522 (= H548), H685 (= H711)
2wgqA Zinc substituted e coli copper amine oxidase, a model for the precursor for 2,4,5-trihydroxyphenylalaninequinone formation
70% identity, 96% coverage: 26:743/748 of query aligns to 1:717/720 of 2wgqA
- active site: Y365 (= Y391), D379 (= D405), Y462 (= Y488), H520 (= H546), H522 (= H548), H685 (= H711)
- binding calcium ion: D529 (= D555), L530 (= L556), D531 (= D557), E569 (= E595), Y663 (≠ F689), D666 (= D692), E668 (≠ Q694), D674 (= D700), A675 (≠ D701)
- binding zinc ion: Y462 (= Y488), H520 (= H546), H522 (= H548), H685 (= H711)
2w0qA E. Coli copper amine oxidase in complex with xenon (see paper)
70% identity, 96% coverage: 28:743/748 of query aligns to 1:715/718 of 2w0qA
- active site: Y363 (= Y391), D377 (= D405), Y460 (= Y488), H518 (= H546), H520 (= H548), H683 (= H711)
- binding calcium ion: D527 (= D555), L528 (= L556), D529 (= D557), E567 (= E595), Y661 (≠ F689), E666 (≠ Q694), D672 (= D700), A673 (≠ D701)
- binding copper (ii) ion: H518 (= H546), H520 (= H548), H683 (= H711)
- binding xenon: V181 (= V208), L182 (= L209), L183 (≠ V210), F186 (= F213), M316 (≠ T344), D323 (≠ E351), F324 (≠ M352), T338 (= T366), Y375 (= Y403), Y381 (= Y409), Y381 (= Y409), S388 (= S416), I390 (= I418), A420 (= A448), W453 (= W481), I454 (= I482), G458 (= G486), L537 (= L565), P542 (= P570), V543 (= V571), M557 (= M585), A570 (= A598), Q572 (= Q600), I599 (≠ L627), L632 (= L660), L632 (= L660)
1d6yA Crystal structure of e. Coli copper-containing amine oxidase anaerobically reduced with beta-phenylethylamine and complexed with nitric oxide. (see paper)
70% identity, 96% coverage: 28:743/748 of query aligns to 1:715/718 of 1d6yA
- active site: Y363 (= Y391), D377 (= D405), Y460 (= Y488), H518 (= H546), H520 (= H548), H683 (= H711)
- binding calcium ion: D527 (= D555), L528 (= L556), D529 (= D557), E567 (= E595), H638 (≠ D666), Y661 (≠ F689), D664 (= D692), D672 (= D700), A673 (≠ D701)
- binding copper (ii) ion: H518 (= H546), H520 (= H548), H683 (= H711)
- binding phenylacetaldehyde: T217 (= T244), P218 (= P245), L219 (= L246), Y375 (= Y403), Y381 (= Y409), G458 (= G486), Y460 (= Y488)
- binding nitric oxide: Y460 (= Y488), H518 (= H546)
- binding 2-phenylethylamine: D96 (= D123), Q100 (≠ A127)
1d6uA Crystal structure of e. Coli amine oxidase anaerobically reduced with beta-phenylethylamine (see paper)
70% identity, 96% coverage: 28:743/748 of query aligns to 1:715/718 of 1d6uA
- active site: Y363 (= Y391), D377 (= D405), Y460 (= Y488), H518 (= H546), H520 (= H548), H683 (= H711)
- binding calcium ion: D527 (= D555), L528 (= L556), D529 (= D557), E567 (= E595), H638 (≠ D666), Y661 (≠ F689), D664 (= D692), D672 (= D700), A673 (≠ D701)
- binding copper (ii) ion: H518 (= H546), H520 (= H548), H683 (= H711)
- binding phenylacetaldehyde: L219 (= L246), Y375 (= Y403), D377 (= D405), Y381 (= Y409), V457 (= V485), G458 (= G486), Y460 (= Y488)
- binding 2-phenylethylamine: D96 (= D123), Q100 (≠ A127)
Q59118 Histamine oxidase; Copper amine oxidase; EC 1.4.3.22 from Arthrobacter globiformis (see paper)
33% identity, 86% coverage: 102:744/748 of query aligns to 15:645/684 of Q59118
- Y402 (= Y488) modified: 2',4',5'-topaquinone
Q43077 Primary amine oxidase; Amine oxidase [copper-containing]; EC 1.4.3.21 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
30% identity, 84% coverage: 113:742/748 of query aligns to 31:659/674 of Q43077
- N156 (≠ D237) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C162 (≠ A243) modified: Disulfide link with 183
- C183 (≠ S268) modified: Disulfide link with 162
- C344 (≠ A424) modified: Disulfide link with 370
- C370 (≠ G450) modified: Disulfide link with 344
- Y412 (= Y488) modified: 2',4',5'-topaquinone
- H467 (= H546) binding
- H469 (= H548) binding
- D476 (= D555) binding
- F477 (≠ L556) binding
- D478 (= D557) binding
- D617 (= D700) binding
- I618 (≠ D701) binding
- H628 (= H711) binding
1w2zA Psao and xenon (see paper)
30% identity, 84% coverage: 113:742/748 of query aligns to 1:629/642 of 1w2zA
- active site: Y281 (= Y391), D295 (= D405), Y382 (= Y488), H437 (= H546), H439 (= H548), H598 (= H711)
- binding copper (ii) ion: H437 (= H546), H439 (= H548), H598 (= H711)
- binding manganese (ii) ion: D446 (= D555), F447 (≠ L556), D448 (= D557), D587 (= D700), I588 (≠ D701)
- binding xenon: L402 (≠ A508), Y441 (= Y550), F447 (≠ L556), Y518 (= Y625), R519 (≠ Q626), L520 (= L627), M590 (≠ V703), T613 (≠ V726)
1ksiA Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2a resolution (see paper)
30% identity, 84% coverage: 113:742/748 of query aligns to 1:629/642 of 1ksiA
- active site: Y281 (= Y391), D295 (= D405), Y382 (= Y488), H437 (= H546), H439 (= H548), H598 (= H711)
- binding copper (ii) ion: H437 (= H546), H439 (= H548), H598 (= H711)
- binding manganese (ii) ion: D446 (= D555), F447 (≠ L556), D448 (= D557), D587 (= D700), I588 (≠ D701)
P46881 Phenylethylamine oxidase; Primary amine oxidase; EC 1.4.3.21 from Arthrobacter globiformis (see paper)
30% identity, 84% coverage: 116:742/748 of query aligns to 11:623/638 of P46881
- C317 (≠ A424) modified: Disulfide link with 343
- C343 (≠ G450) modified: Disulfide link with 317
- Y382 (= Y488) modified: 2',4',5'-topaquinone
- H431 (= H546) binding
- H433 (= H548) binding
- H592 (= H711) binding
8j6gA Neutron structure of copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at pd 9.0
30% identity, 84% coverage: 116:742/748 of query aligns to 4:616/621 of 8j6gA
3wa2X High resolution crystal structure of copper amine oxidase from arthrobacter globiformis (see paper)
30% identity, 84% coverage: 116:742/748 of query aligns to 3:615/621 of 3wa2X
- binding copper (ii) ion: H423 (= H546), H425 (= H548), H584 (= H711)
- binding 1,2-ethanediol: Y33 (≠ E146), G35 (≠ T148), V36 (≠ L149), L37 (≠ A150), R53 (= R172), R109 (≠ E225), R180 (≠ K298), V181 (≠ I299), D242 (= D357), W341 (≠ A456), I343 (≠ P458), N355 (= N469), Y356 (≠ L470), R358 (≠ V472), N360 (≠ R474), E405 (≠ D524), G407 (≠ S526), Q450 (≠ L573), P454 (= P577), G455 (= G578), G455 (= G578), E457 (≠ P580), R524 (≠ K651), A527 (≠ S654), R543 (= R670), Y544 (≠ F671), G556 (≠ D683)
- binding oxygen molecule: L148 (≠ V267), A149 (≠ S268), V164 (≠ I282), L167 (= L285), E391 (≠ N505), H509 (≠ Y630), T513 (= T634), L514 (≠ H635), T530 (≠ D657)
5zpnA Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 8 at 288 k (1) (see paper)
30% identity, 84% coverage: 116:742/748 of query aligns to 3:615/620 of 5zpnA
- active site: Y276 (= Y391), D290 (= D405), Y374 (= Y488), H423 (= H546), H425 (= H548), H584 (= H711)
- binding copper (ii) ion: H423 (= H546), H425 (= H548), H584 (= H711)
- binding phenylacetaldehyde: L129 (= L246), Y288 (= Y403), D290 (= D405), Y294 (= Y409), I371 (≠ V485), G372 (= G486), Y374 (= Y488)
3x3xA Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine (see paper)
30% identity, 84% coverage: 116:742/748 of query aligns to 3:615/620 of 3x3xA
- active site: Y276 (= Y391), D290 (= D405), Y374 (= Y488), H423 (= H546), H425 (= H548), H584 (= H711)
- binding copper (ii) ion: H423 (= H546), H425 (= H548), H584 (= H711)
- binding glycerol: I31 (≠ F144), Y33 (≠ E146), V243 (≠ S358), S321 (≠ A436), D322 (= D437), R362 (≠ E476), E389 (≠ G503), E391 (≠ N505)
- binding 2-phenyl-ethanol: P128 (= P245), L129 (= L246), Y288 (= Y403), D290 (= D405), Y294 (= Y409), I371 (≠ V485), G372 (= G486), N373 (= N487)
2cg1A Agao in complex with wc11b (ru-wire inhibitor, 11-carbon linker, data set b) (see paper)
30% identity, 84% coverage: 116:742/748 of query aligns to 3:615/620 of 2cg1A
- active site: Y276 (= Y391), D290 (= D405), Y374 (= Y488), H423 (= H546), H425 (= H548), H584 (= H711)
- binding ruthenium wire, 11 carbon linker: F97 (vs. gap), P128 (= P245), L129 (= L246), Y288 (= Y403), Y294 (= Y409), Y299 (≠ L414), T370 (= T484), G372 (= G486), Y374 (= Y488)
- binding copper (ii) ion: H423 (= H546), H425 (= H548), H584 (= H711)
2cg0A Agao in complex with wc9a (ru-wire inhibitor, 9-carbon linker, data set a) (see paper)
30% identity, 84% coverage: 116:742/748 of query aligns to 3:615/620 of 2cg0A
- active site: Y276 (= Y391), D290 (= D405), Y374 (= Y488), H423 (= H546), H425 (= H548), H584 (= H711)
- binding copper (ii) ion: H423 (= H546), H425 (= H548), H584 (= H711)
- binding ruthenium wire, 9 carbon linker: F97 (vs. gap), L129 (= L246), Y288 (= Y403), Y294 (= Y409), Y299 (≠ L414), G372 (= G486), Y374 (= Y488)
2cfwA Agao in complex with wc7a (ru-wire inhibitor, 7-carbon linker, data set a) (see paper)
30% identity, 84% coverage: 116:742/748 of query aligns to 3:615/620 of 2cfwA
- active site: Y276 (= Y391), D290 (= D405), Y374 (= Y488), H423 (= H546), H425 (= H548), H584 (= H711)
- binding copper (ii) ion: H423 (= H546), H425 (= H548), H584 (= H711)
- binding ruthenium wire, 7 carbon linker: F97 (vs. gap), P128 (= P245), L129 (= L246), Y288 (= Y403), Y294 (= Y409), Y299 (≠ L414), A300 (≠ T415), G372 (= G486), Y374 (= Y488)
2cflA Agao in complex with wc6b (ru-wire inhibitor, 6-carbon linker, data set b) (see paper)
30% identity, 84% coverage: 116:742/748 of query aligns to 3:615/620 of 2cflA
- active site: Y276 (= Y391), D290 (= D405), Y374 (= Y488), H423 (= H546), H425 (= H548), H584 (= H711)
- binding copper (ii) ion: H423 (= H546), H425 (= H548), H584 (= H711)
- binding ruthenium wire, 6 carbon linker: E94 (vs. gap), F97 (vs. gap), L129 (= L246), Y288 (= Y403), Y294 (= Y409), G372 (= G486), Y374 (= Y488)
2cfkA Agao in complex with wc5 (ru-wire inhibitor, 5-carbon linker) (see paper)
30% identity, 84% coverage: 116:742/748 of query aligns to 3:615/620 of 2cfkA
- active site: Y276 (= Y391), D290 (= D405), Y374 (= Y488), H423 (= H546), H425 (= H548), H584 (= H711)
- binding copper (ii) ion: H423 (= H546), H425 (= H548), H584 (= H711)
- binding ruthenium wire, 5 carbon linker: E94 (vs. gap), F97 (vs. gap), P128 (= P245), L129 (= L246), Y288 (= Y403), Y294 (= Y409), Y299 (≠ L414), T370 (= T484), G372 (= G486), Y374 (= Y488)
- binding ruthenium wire wc5: E94 (vs. gap), F97 (vs. gap), E98 (vs. gap), P128 (= P245), L129 (= L246), Y288 (= Y403), Y294 (= Y409), R328 (= R443), G372 (= G486), Y374 (= Y488)
Query Sequence
>HSERO_RS17625 FitnessBrowser__HerbieS:HSERO_RS17625
LTTLTAAGLSTALLGPLPAAAHGAAAHMLPLKKTMEDFGATVRWDAYAGLWTIQRNSVTV
RVKPRATTALVNGQSVKLPVPLVMKGGQPYVSDEFINTVFAPSLDKTFQIEAVPHPLNPL
SADEINAALEVLKASGRWQPNYRFTEITLAEPPKEQVWKFALGERGQTIARRADFTLLDG
SKVIEGTVDLGQRNVTRWEPKEGVHGMVLVDDFATVQNAMESSPEYAQALAKRGITDIKK
VVATPLTVGYFGGKDALQEDARLLKVVSYLDVGDGNYWAHPIENLVAVVDLVQKKVIKIE
DNGVIPVPMKPTGYDGSGRALVPPPKPLDISEPEGKNYTITGNTLRWRNWEMHFKLDSRV
GLMFSTVTYNDHGKKRQIMYEGSLGGMIVPYGDPDVGWYFKAYLDSGEYGMGTLTSPIER
GKDAPDNVVLLDATLADTSGKPRTIPRAIGVFERYAGPEFKHQEYGQPNLSVERRELVIR
WISTVGNYDYIFDWVFAENGTIGINAGATGIEAVKGVKSSTMRDASAAEDTRYGTLIDHN
IVGTTHQHIYNFRLDLDVDGQNNSLTEVDPVVLPNTPGGPRSSTMQTVQRTAETEQQAAQ
KFDASTIRLLSNPNKFNKVGNPVSYQLIPYAGGTHPIAKGANFSPDEWLNKRLSFMDRQL
WVTRYDPQQRFPEGKYPNRSHEDTGLGAFVKDNQSIVNQDDVVWLTTGTTHVARAEEWPI
MPTEWVHVLLKPWNFFDETPTLGLNKKK
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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