SitesBLAST
Comparing PfGW456L13_2439 Monoamine oxidase (1.4.3.4) 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)
71% identity, 99% coverage: 1:756/762 of query aligns to 1:750/757 of P46883
- 1:30 (vs. 1:36, 25% identical) signal peptide
- 411:422 (vs. 417:428, 100% identical) binding
- D413 (= D419) active site, Proton acceptor
- VGNYDY 493:498 (= VGNYDY 499:504) binding
- Y496 (= Y502) active site, Schiff-base intermediate with substrate; via topaquinone; modified: 2',4',5'-topaquinone
- H554 (= H560) binding
- H556 (= H562) binding
- D563 (= D569) binding
- L564 (≠ M570) binding
- D565 (= D571) binding
- E603 (= E609) binding
- Y697 (≠ F703) binding
- D700 (= D706) binding
- E702 (≠ H708) binding
- D708 (= D714) binding
- A709 (≠ D715) binding
- H719 (= H725) binding
2wgqA Zinc substituted e coli copper amine oxidase, a model for the precursor for 2,4,5-trihydroxyphenylalaninequinone formation
73% identity, 94% coverage: 41:756/762 of query aligns to 1:716/720 of 2wgqA
- active site: Y365 (= Y405), D379 (= D419), Y462 (= Y502), H520 (= H560), H522 (= H562), H685 (= H725)
- binding calcium ion: D529 (= D569), L530 (≠ M570), D531 (= D571), E569 (= E609), Y663 (≠ F703), D666 (= D706), E668 (≠ H708), D674 (= D714), A675 (≠ D715)
- binding zinc ion: Y462 (= Y502), H520 (= H560), H522 (= H562), H685 (= H725)
1oacB Crystal structure of a quinoenzyme: copper amine oxidase of escherichia coli at 2 angstroems resolution (see paper)
73% identity, 94% coverage: 41:756/762 of query aligns to 1:716/723 of 1oacB
- active site: Y365 (= Y405), D379 (= D419), Y462 (= Y502), H520 (= H560), H522 (= H562), H685 (= H725)
- binding calcium ion: D529 (= D569), L530 (≠ M570), D531 (= D571), E569 (= E609), Y663 (≠ F703), D666 (= D706), E668 (≠ H708), D674 (= D714), A675 (≠ D715)
- binding copper (ii) ion: Y462 (= Y502), H520 (= H560), H522 (= H562), H685 (= H725)
2w0qA E. Coli copper amine oxidase in complex with xenon (see paper)
73% identity, 94% coverage: 43:756/762 of query aligns to 1:714/718 of 2w0qA
- active site: Y363 (= Y405), D377 (= D419), Y460 (= Y502), H518 (= H560), H520 (= H562), H683 (= H725)
- binding calcium ion: D527 (= D569), L528 (≠ M570), D529 (= D571), E567 (= E609), Y661 (≠ F703), E666 (≠ H708), D672 (= D714), A673 (≠ D715)
- binding copper (ii) ion: H518 (= H560), H520 (= H562), H683 (= H725)
- binding xenon: V181 (= V223), L182 (= L224), L183 (= L225), F186 (= F228), M316 (≠ S358), D323 (= D365), F324 (= F366), T338 (= T380), Y375 (= Y417), Y381 (= Y423), Y381 (= Y423), S388 (= S430), I390 (= I432), A420 (= A462), W453 (= W495), I454 (= I496), G458 (= G500), L537 (= L579), P542 (= P584), V543 (= V585), M557 (= M599), A570 (= A612), Q572 (= Q614), I599 (≠ L641), L632 (= L674), L632 (= L674)
1d6yA Crystal structure of e. Coli copper-containing amine oxidase anaerobically reduced with beta-phenylethylamine and complexed with nitric oxide. (see paper)
73% identity, 94% coverage: 43:756/762 of query aligns to 1:714/718 of 1d6yA
- active site: Y363 (= Y405), D377 (= D419), Y460 (= Y502), H518 (= H560), H520 (= H562), H683 (= H725)
- binding calcium ion: D527 (= D569), L528 (≠ M570), D529 (= D571), E567 (= E609), H638 (≠ N680), Y661 (≠ F703), D664 (= D706), D672 (= D714), A673 (≠ D715)
- binding copper (ii) ion: H518 (= H560), H520 (= H562), H683 (= H725)
- binding phenylacetaldehyde: T217 (= T259), P218 (= P260), L219 (= L261), Y375 (= Y417), Y381 (= Y423), G458 (= G500), Y460 (= Y502)
- binding nitric oxide: Y460 (= Y502), H518 (= H560)
- binding 2-phenylethylamine: D96 (≠ A138), Q100 (≠ T142)
1d6uA Crystal structure of e. Coli amine oxidase anaerobically reduced with beta-phenylethylamine (see paper)
73% identity, 94% coverage: 43:756/762 of query aligns to 1:714/718 of 1d6uA
- active site: Y363 (= Y405), D377 (= D419), Y460 (= Y502), H518 (= H560), H520 (= H562), H683 (= H725)
- binding calcium ion: D527 (= D569), L528 (≠ M570), D529 (= D571), E567 (= E609), H638 (≠ N680), Y661 (≠ F703), D664 (= D706), D672 (= D714), A673 (≠ D715)
- binding copper (ii) ion: H518 (= H560), H520 (= H562), H683 (= H725)
- binding phenylacetaldehyde: L219 (= L261), Y375 (= Y417), D377 (= D419), Y381 (= Y423), V457 (= V499), G458 (= G500), Y460 (= Y502)
- binding 2-phenylethylamine: D96 (≠ A138), Q100 (≠ T142)
Q59118 Histamine oxidase; Copper amine oxidase; EC 1.4.3.22 from Arthrobacter globiformis (see paper)
32% identity, 84% coverage: 122:760/762 of query aligns to 20:647/684 of Q59118
- Y402 (= Y502) 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)
31% identity, 83% coverage: 130:762/762 of query aligns to 33:665/674 of Q43077
- N156 (= N251) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C162 (≠ A258) modified: Disulfide link with 183
- C183 (≠ S283) modified: Disulfide link with 162
- C344 (≠ A438) modified: Disulfide link with 370
- C370 (≠ A464) modified: Disulfide link with 344
- Y412 (= Y502) modified: 2',4',5'-topaquinone
- H467 (= H560) binding
- H469 (= H562) binding
- D476 (= D569) binding
- F477 (≠ M570) binding
- D478 (= D571) binding
- D617 (= D714) binding
- I618 (≠ D715) binding
- H628 (= H725) binding
1w2zA Psao and xenon (see paper)
31% identity, 83% coverage: 130:762/762 of query aligns to 3:635/642 of 1w2zA
- active site: Y281 (= Y405), D295 (= D419), Y382 (= Y502), H437 (= H560), H439 (= H562), H598 (= H725)
- binding copper (ii) ion: H437 (= H560), H439 (= H562), H598 (= H725)
- binding manganese (ii) ion: D446 (= D569), F447 (≠ M570), D448 (= D571), D587 (= D714), I588 (≠ D715)
- binding xenon: L402 (≠ A522), Y441 (= Y564), F447 (≠ M570), Y518 (= Y639), R519 (≠ Q640), L520 (= L641), M590 (≠ V717), T613 (≠ V740)
1ksiA Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2a resolution (see paper)
31% identity, 83% coverage: 130:762/762 of query aligns to 3:635/642 of 1ksiA
- active site: Y281 (= Y405), D295 (= D419), Y382 (= Y502), H437 (= H560), H439 (= H562), H598 (= H725)
- binding copper (ii) ion: H437 (= H560), H439 (= H562), H598 (= H725)
- binding manganese (ii) ion: D446 (= D569), F447 (≠ M570), D448 (= D571), D587 (= D714), I588 (≠ D715)
8j6gA Neutron structure of copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at pd 9.0
30% identity, 83% coverage: 130:758/762 of query aligns to 3:618/621 of 8j6gA
3wa2X High resolution crystal structure of copper amine oxidase from arthrobacter globiformis (see paper)
30% identity, 83% coverage: 130:758/762 of query aligns to 2:617/621 of 3wa2X
- binding copper (ii) ion: H423 (= H560), H425 (= H562), H584 (= H725)
- binding 1,2-ethanediol: Y33 (≠ E161), G35 (≠ S163), V36 (= V164), L37 (≠ K165), R53 (≠ N174), R109 (≠ E240), R180 (≠ K313), V181 (≠ I314), D242 (= D371), W341 (≠ A470), I343 (≠ P472), N355 (= N483), Y356 (≠ L484), R358 (≠ T486), N360 (≠ R488), E405 (= E538), G407 (≠ T540), Q450 (≠ L587), P454 (≠ R591), G455 (= G592), G455 (= G592), E457 (≠ P594), R524 (≠ K659), A527 (≠ S668), R543 (≠ K684), Y544 (= Y685), G556 (≠ D697)
- binding oxygen molecule: L148 (≠ V282), A149 (≠ S283), V164 (≠ I297), L167 (= L300), E391 (≠ D519), H509 (≠ Y644), T513 (= T648), L514 (≠ H649), T530 (≠ D671)
P46881 Phenylethylamine oxidase; Primary amine oxidase; EC 1.4.3.21 from Arthrobacter globiformis (see paper)
30% identity, 83% coverage: 130:758/762 of query aligns to 10:625/638 of P46881
- C317 (≠ A438) modified: Disulfide link with 343
- C343 (≠ A464) modified: Disulfide link with 317
- Y382 (= Y502) modified: 2',4',5'-topaquinone
- H431 (= H560) binding
- H433 (= H562) binding
- H592 (= H725) binding
5zpnA Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 8 at 288 k (1) (see paper)
30% identity, 83% coverage: 130:758/762 of query aligns to 2:617/620 of 5zpnA
- active site: Y276 (= Y405), D290 (= D419), Y374 (= Y502), H423 (= H560), H425 (= H562), H584 (= H725)
- binding copper (ii) ion: H423 (= H560), H425 (= H562), H584 (= H725)
- binding phenylacetaldehyde: L129 (= L261), Y288 (= Y417), D290 (= D419), Y294 (= Y423), I371 (≠ V499), G372 (= G500), Y374 (= Y502)
3x3xA Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine (see paper)
30% identity, 83% coverage: 130:758/762 of query aligns to 2:617/620 of 3x3xA
- active site: Y276 (= Y405), D290 (= D419), Y374 (= Y502), H423 (= H560), H425 (= H562), H584 (= H725)
- binding copper (ii) ion: H423 (= H560), H425 (= H562), H584 (= H725)
- binding glycerol: I31 (≠ F159), Y33 (≠ E161), V243 (≠ S372), S321 (≠ A450), D322 (= D451), R362 (≠ E490), E389 (≠ G517), E391 (≠ D519)
- binding 2-phenyl-ethanol: P128 (= P260), L129 (= L261), Y288 (= Y417), D290 (= D419), Y294 (= Y423), I371 (≠ V499), G372 (= G500), N373 (= N501)
2cg1A Agao in complex with wc11b (ru-wire inhibitor, 11-carbon linker, data set b) (see paper)
30% identity, 83% coverage: 130:758/762 of query aligns to 2:617/620 of 2cg1A
- active site: Y276 (= Y405), D290 (= D419), Y374 (= Y502), H423 (= H560), H425 (= H562), H584 (= H725)
- binding ruthenium wire, 11 carbon linker: F97 (≠ E217), P128 (= P260), L129 (= L261), Y288 (= Y417), Y294 (= Y423), Y299 (≠ L428), T370 (= T498), G372 (= G500), Y374 (= Y502)
- binding copper (ii) ion: H423 (= H560), H425 (= H562), H584 (= H725)
2cg0A Agao in complex with wc9a (ru-wire inhibitor, 9-carbon linker, data set a) (see paper)
30% identity, 83% coverage: 130:758/762 of query aligns to 2:617/620 of 2cg0A
- active site: Y276 (= Y405), D290 (= D419), Y374 (= Y502), H423 (= H560), H425 (= H562), H584 (= H725)
- binding copper (ii) ion: H423 (= H560), H425 (= H562), H584 (= H725)
- binding ruthenium wire, 9 carbon linker: F97 (≠ E217), L129 (= L261), Y288 (= Y417), Y294 (= Y423), Y299 (≠ L428), G372 (= G500), Y374 (= Y502)
2cfwA Agao in complex with wc7a (ru-wire inhibitor, 7-carbon linker, data set a) (see paper)
30% identity, 83% coverage: 130:758/762 of query aligns to 2:617/620 of 2cfwA
- active site: Y276 (= Y405), D290 (= D419), Y374 (= Y502), H423 (= H560), H425 (= H562), H584 (= H725)
- binding copper (ii) ion: H423 (= H560), H425 (= H562), H584 (= H725)
- binding ruthenium wire, 7 carbon linker: F97 (≠ E217), P128 (= P260), L129 (= L261), Y288 (= Y417), Y294 (= Y423), Y299 (≠ L428), A300 (≠ T429), G372 (= G500), Y374 (= Y502)
2cflA Agao in complex with wc6b (ru-wire inhibitor, 6-carbon linker, data set b) (see paper)
30% identity, 83% coverage: 130:758/762 of query aligns to 2:617/620 of 2cflA
- active site: Y276 (= Y405), D290 (= D419), Y374 (= Y502), H423 (= H560), H425 (= H562), H584 (= H725)
- binding copper (ii) ion: H423 (= H560), H425 (= H562), H584 (= H725)
- binding ruthenium wire, 6 carbon linker: E94 (≠ K214), F97 (≠ E217), L129 (= L261), Y288 (= Y417), Y294 (= Y423), G372 (= G500), Y374 (= Y502)
2cfkA Agao in complex with wc5 (ru-wire inhibitor, 5-carbon linker) (see paper)
30% identity, 83% coverage: 130:758/762 of query aligns to 2:617/620 of 2cfkA
- active site: Y276 (= Y405), D290 (= D419), Y374 (= Y502), H423 (= H560), H425 (= H562), H584 (= H725)
- binding copper (ii) ion: H423 (= H560), H425 (= H562), H584 (= H725)
- binding ruthenium wire, 5 carbon linker: E94 (≠ K214), F97 (≠ E217), P128 (= P260), L129 (= L261), Y288 (= Y417), Y294 (= Y423), Y299 (≠ L428), T370 (= T498), G372 (= G500), Y374 (= Y502)
- binding ruthenium wire wc5: E94 (≠ K214), F97 (≠ E217), E98 (≠ G218), P128 (= P260), L129 (= L261), Y288 (= Y417), Y294 (= Y423), R328 (≠ T457), G372 (= G500), Y374 (= Y502)
Query Sequence
>PfGW456L13_2439 Monoamine oxidase (1.4.3.4)
MFSPKASPKRTPLARLALAITLSTLGLPFWAGNAQAHGGHAEMVPLQAGLEEFGATVKWD
DYANLFTIAKDGVYLKVKPDSKVAMLNGKRIELTVPVVFKDHTAFMSKDFINQVFQSGLD
KTFVVETRPNPLNPLSAAEITTAVDIVKKSENYKPGFRFTEVSVKEPPKDQVWNFALTGQ
NVAQPRQASIVVLDGKHVIEAQVDLDTKELKSWKPIEGAHGMVLLDDFATVQTAVETSPE
YAQALAKRGINDVKKVVATPLTVGFFDGKDGLAQDKRLLKIVSYLNTGDGNYWAHPIEGL
VAIVDLEQKKLIKIEDDALIPVPMNPTPYDGRGRQGVAVKPLEIIEPEGKNYTISGNSIH
WQNWDFHVRLDSRVGPILSTVTYDDKGKKRKIMYEGSLGGMIVPYGDPDVGWYFKAYLDS
GDYGMGTLTSPIARGKDAPQNAVLLDATIADYTGTPTAIPRAMAVFERYAGPEYKHQEMG
QPNLSTERRELVVRWISTVGNYDYIFDWVFQQNGTIGIDAGATGIEAVKGVKSKTMHEDT
AREDTRYGTLLDHNIVGTTHQHIYNFRLDMDVDGEQNSLVEVNPVVLPNDRGGPRTSTMQ
TETKVVGNEQQAAQKFDPSTVRLLTNFSKENKVGNPVSYQLIPYAGGTHPVAKGANFGKD
EWLYHRLSFMDKQLWVTQYNPEEKYPEGKYPNRSDKDSGLGQFTQDNHSIENTDDVVWLT
TGTTHIARAEEWPIMPTEWVHVLLKPWNFFDETPTLNLSSPK
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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