SitesBLAST
Comparing BWI76_RS13080 FitnessBrowser__Koxy:BWI76_RS13080 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)
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)
87% identity, 100% coverage: 2:752/752 of query aligns to 5:755/757 of P46883
- 411:422 (vs. 408:419, 100% identical) binding
- D413 (= D410) active site, Proton acceptor
- VGNYDY 493:498 (= VGNYDY 490:495) binding
- Y496 (= Y493) active site, Schiff-base intermediate with substrate; via topaquinone; modified: 2',4',5'-topaquinone
- H554 (= H551) binding
- H556 (= H553) binding
- D563 (= D560) binding
- L564 (= L561) binding
- D565 (= D562) binding
- E603 (= E600) binding
- Y697 (= Y694) binding
- D700 (= D697) binding
- E702 (= E699) binding
- D708 (= D705) binding
- A709 (≠ D706) binding
- H719 (= H716) 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)
87% identity, 96% coverage: 32:752/752 of query aligns to 1:721/723 of 1oacB
- active site: Y365 (= Y396), D379 (= D410), Y462 (= Y493), H520 (= H551), H522 (= H553), H685 (= H716)
- binding calcium ion: D529 (= D560), L530 (= L561), D531 (= D562), E569 (= E600), Y663 (= Y694), D666 (= D697), E668 (= E699), D674 (= D705), A675 (≠ D706)
- binding copper (ii) ion: Y462 (= Y493), H520 (= H551), H522 (= H553), H685 (= H716)
2wgqA Zinc substituted e coli copper amine oxidase, a model for the precursor for 2,4,5-trihydroxyphenylalaninequinone formation
88% identity, 96% coverage: 32:751/752 of query aligns to 1:720/720 of 2wgqA
- active site: Y365 (= Y396), D379 (= D410), Y462 (= Y493), H520 (= H551), H522 (= H553), H685 (= H716)
- binding calcium ion: D529 (= D560), L530 (= L561), D531 (= D562), E569 (= E600), Y663 (= Y694), D666 (= D697), E668 (= E699), D674 (= D705), A675 (≠ D706)
- binding zinc ion: Y462 (= Y493), H520 (= H551), H522 (= H553), H685 (= H716)
2w0qA E. Coli copper amine oxidase in complex with xenon (see paper)
87% identity, 95% coverage: 34:751/752 of query aligns to 1:718/718 of 2w0qA
- active site: Y363 (= Y396), D377 (= D410), Y460 (= Y493), H518 (= H551), H520 (= H553), H683 (= H716)
- binding calcium ion: D527 (= D560), L528 (= L561), D529 (= D562), E567 (= E600), Y661 (= Y694), E666 (= E699), D672 (= D705), A673 (≠ D706)
- binding copper (ii) ion: H518 (= H551), H520 (= H553), H683 (= H716)
- binding xenon: V181 (= V214), L182 (= L215), L183 (= L216), F186 (= F219), M316 (= M349), D323 (= D356), F324 (= F357), T338 (= T371), Y375 (= Y408), Y381 (= Y414), Y381 (= Y414), S388 (= S421), I390 (= I423), A420 (= A453), W453 (= W486), I454 (= I487), G458 (= G491), L537 (= L570), P542 (= P575), V543 (≠ E576), M557 (= M590), A570 (= A603), Q572 (= Q605), I599 (= I632), L632 (= L665), L632 (= L665)
1d6yA Crystal structure of e. Coli copper-containing amine oxidase anaerobically reduced with beta-phenylethylamine and complexed with nitric oxide. (see paper)
87% identity, 95% coverage: 34:751/752 of query aligns to 1:718/718 of 1d6yA
- active site: Y363 (= Y396), D377 (= D410), Y460 (= Y493), H518 (= H551), H520 (= H553), H683 (= H716)
- binding calcium ion: D527 (= D560), L528 (= L561), D529 (= D562), E567 (= E600), H638 (= H671), Y661 (= Y694), D664 (= D697), D672 (= D705), A673 (≠ D706)
- binding copper (ii) ion: H518 (= H551), H520 (= H553), H683 (= H716)
- binding phenylacetaldehyde: T217 (= T250), P218 (= P251), L219 (= L252), Y375 (= Y408), Y381 (= Y414), G458 (= G491), Y460 (= Y493)
- binding nitric oxide: Y460 (= Y493), H518 (= H551)
- binding 2-phenylethylamine: D96 (≠ A129), Q100 (≠ A133)
1d6uA Crystal structure of e. Coli amine oxidase anaerobically reduced with beta-phenylethylamine (see paper)
87% identity, 95% coverage: 34:751/752 of query aligns to 1:718/718 of 1d6uA
- active site: Y363 (= Y396), D377 (= D410), Y460 (= Y493), H518 (= H551), H520 (= H553), H683 (= H716)
- binding calcium ion: D527 (= D560), L528 (= L561), D529 (= D562), E567 (= E600), H638 (= H671), Y661 (= Y694), D664 (= D697), D672 (= D705), A673 (≠ D706)
- binding copper (ii) ion: H518 (= H551), H520 (= H553), H683 (= H716)
- binding phenylacetaldehyde: L219 (= L252), Y375 (= Y408), D377 (= D410), Y381 (= Y414), V457 (= V490), G458 (= G491), Y460 (= Y493)
- binding 2-phenylethylamine: D96 (≠ A129), Q100 (≠ A133)
Q59118 Histamine oxidase; Copper amine oxidase; EC 1.4.3.22 from Arthrobacter globiformis (see paper)
32% identity, 83% coverage: 121:747/752 of query aligns to 28:643/684 of Q59118
- Y402 (= Y493) 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, 83% coverage: 121:747/752 of query aligns to 33:659/674 of Q43077
- N156 (≠ D242) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C162 (≠ T249) modified: Disulfide link with 183
- C183 (≠ S274) modified: Disulfide link with 162
- C344 (≠ A429) modified: Disulfide link with 370
- C370 (≠ A455) modified: Disulfide link with 344
- Y412 (= Y493) modified: 2',4',5'-topaquinone
- H467 (= H551) binding
- H469 (= H553) binding
- D476 (= D560) binding
- F477 (≠ L561) binding
- D478 (= D562) binding
- D617 (= D705) binding
- I618 (≠ D706) binding
- H628 (= H716) binding
1w2zA Psao and xenon (see paper)
30% identity, 83% coverage: 121:747/752 of query aligns to 3:629/642 of 1w2zA
- active site: Y281 (= Y396), D295 (= D410), Y382 (= Y493), H437 (= H551), H439 (= H553), H598 (= H716)
- binding copper (ii) ion: H437 (= H551), H439 (= H553), H598 (= H716)
- binding manganese (ii) ion: D446 (= D560), F447 (≠ L561), D448 (= D562), D587 (= D705), I588 (≠ D706)
- binding xenon: L402 (≠ A513), Y441 (= Y555), F447 (≠ L561), Y518 (= Y630), R519 (≠ Q631), L520 (≠ I632), M590 (≠ V708), T613 (≠ A731)
1ksiA Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2a resolution (see paper)
30% identity, 83% coverage: 121:747/752 of query aligns to 3:629/642 of 1ksiA
- active site: Y281 (= Y396), D295 (= D410), Y382 (= Y493), H437 (= H551), H439 (= H553), H598 (= H716)
- binding copper (ii) ion: H437 (= H551), H439 (= H553), H598 (= H716)
- binding manganese (ii) ion: D446 (= D560), F447 (≠ L561), D448 (= D562), D587 (= D705), I588 (≠ D706)
3wa2X High resolution crystal structure of copper amine oxidase from arthrobacter globiformis (see paper)
29% identity, 83% coverage: 122:747/752 of query aligns to 3:615/621 of 3wa2X
- binding copper (ii) ion: H423 (= H551), H425 (= H553), H584 (= H716)
- binding 1,2-ethanediol: Y33 (≠ E152), G35 (≠ S154), V36 (≠ L155), L37 (≠ R156), R53 (≠ A179), R109 (≠ E231), R180 (≠ K304), V181 (≠ I305), D242 (≠ N362), W341 (≠ A461), I343 (≠ P463), N355 (= N474), Y356 (≠ V475), R358 (≠ T477), N360 (≠ R479), E405 (≠ S531), G407 (≠ K533), Q450 (≠ K578), P454 (≠ A582), G455 (= G583), G455 (= G583), E457 (≠ P585), R524 (≠ H656), A527 (≠ S659), R543 (= R675), Y544 (≠ F676), G556 (≠ D688)
- binding oxygen molecule: L148 (≠ V273), A149 (≠ S274), V164 (≠ I288), L167 (= L291), E391 (≠ D510), H509 (≠ Y635), T513 (= T639), L514 (≠ H640), T530 (≠ D662)
P46881 Phenylethylamine oxidase; Primary amine oxidase; EC 1.4.3.21 from Arthrobacter globiformis (see paper)
29% identity, 83% coverage: 122:747/752 of query aligns to 11:623/638 of P46881
- C317 (≠ A429) modified: Disulfide link with 343
- C343 (≠ A455) modified: Disulfide link with 317
- Y382 (= Y493) modified: 2',4',5'-topaquinone
- H431 (= H551) binding
- H433 (= H553) binding
- H592 (= H716) binding
5zpnA Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 8 at 288 k (1) (see paper)
29% identity, 83% coverage: 122:747/752 of query aligns to 3:615/620 of 5zpnA
- active site: Y276 (= Y396), D290 (= D410), Y374 (= Y493), H423 (= H551), H425 (= H553), H584 (= H716)
- binding copper (ii) ion: H423 (= H551), H425 (= H553), H584 (= H716)
- binding phenylacetaldehyde: L129 (= L252), Y288 (= Y408), D290 (= D410), Y294 (= Y414), I371 (≠ V490), G372 (= G491), Y374 (= Y493)
3x3xA Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine (see paper)
29% identity, 83% coverage: 122:747/752 of query aligns to 3:615/620 of 3x3xA
- active site: Y276 (= Y396), D290 (= D410), Y374 (= Y493), H423 (= H551), H425 (= H553), H584 (= H716)
- binding copper (ii) ion: H423 (= H551), H425 (= H553), H584 (= H716)
- binding glycerol: I31 (≠ F150), Y33 (≠ E152), V243 (≠ S363), S321 (≠ A441), D322 (= D442), R362 (≠ E481), E389 (≠ G508), E391 (≠ D510)
- binding 2-phenyl-ethanol: P128 (= P251), L129 (= L252), Y288 (= Y408), D290 (= D410), Y294 (= Y414), I371 (≠ V490), G372 (= G491), N373 (= N492)
2cg1A Agao in complex with wc11b (ru-wire inhibitor, 11-carbon linker, data set b) (see paper)
29% identity, 83% coverage: 122:747/752 of query aligns to 3:615/620 of 2cg1A
- active site: Y276 (= Y396), D290 (= D410), Y374 (= Y493), H423 (= H551), H425 (= H553), H584 (= H716)
- binding ruthenium wire, 11 carbon linker: F97 (= F219), P128 (= P251), L129 (= L252), Y288 (= Y408), Y294 (= Y414), Y299 (≠ L419), T370 (= T489), G372 (= G491), Y374 (= Y493)
- binding copper (ii) ion: H423 (= H551), H425 (= H553), H584 (= H716)
2cg0A Agao in complex with wc9a (ru-wire inhibitor, 9-carbon linker, data set a) (see paper)
29% identity, 83% coverage: 122:747/752 of query aligns to 3:615/620 of 2cg0A
- active site: Y276 (= Y396), D290 (= D410), Y374 (= Y493), H423 (= H551), H425 (= H553), H584 (= H716)
- binding copper (ii) ion: H423 (= H551), H425 (= H553), H584 (= H716)
- binding ruthenium wire, 9 carbon linker: F97 (= F219), L129 (= L252), Y288 (= Y408), Y294 (= Y414), Y299 (≠ L419), G372 (= G491), Y374 (= Y493)
2cfwA Agao in complex with wc7a (ru-wire inhibitor, 7-carbon linker, data set a) (see paper)
29% identity, 83% coverage: 122:747/752 of query aligns to 3:615/620 of 2cfwA
- active site: Y276 (= Y396), D290 (= D410), Y374 (= Y493), H423 (= H551), H425 (= H553), H584 (= H716)
- binding copper (ii) ion: H423 (= H551), H425 (= H553), H584 (= H716)
- binding ruthenium wire, 7 carbon linker: F97 (= F219), P128 (= P251), L129 (= L252), Y288 (= Y408), Y294 (= Y414), Y299 (≠ L419), A300 (≠ T420), G372 (= G491), Y374 (= Y493)
2cflA Agao in complex with wc6b (ru-wire inhibitor, 6-carbon linker, data set b) (see paper)
29% identity, 83% coverage: 122:747/752 of query aligns to 3:615/620 of 2cflA
- active site: Y276 (= Y396), D290 (= D410), Y374 (= Y493), H423 (= H551), H425 (= H553), H584 (= H716)
- binding copper (ii) ion: H423 (= H551), H425 (= H553), H584 (= H716)
- binding ruthenium wire, 6 carbon linker: E94 (≠ L216), F97 (= F219), L129 (= L252), Y288 (= Y408), Y294 (= Y414), G372 (= G491), Y374 (= Y493)
2cfkA Agao in complex with wc5 (ru-wire inhibitor, 5-carbon linker) (see paper)
29% identity, 83% coverage: 122:747/752 of query aligns to 3:615/620 of 2cfkA
- active site: Y276 (= Y396), D290 (= D410), Y374 (= Y493), H423 (= H551), H425 (= H553), H584 (= H716)
- binding copper (ii) ion: H423 (= H551), H425 (= H553), H584 (= H716)
- binding ruthenium wire, 5 carbon linker: E94 (≠ L216), F97 (= F219), P128 (= P251), L129 (= L252), Y288 (= Y408), Y294 (= Y414), Y299 (≠ L419), T370 (= T489), G372 (= G491), Y374 (= Y493)
- binding ruthenium wire wc5: E94 (≠ L216), F97 (= F219), E98 (≠ A220), P128 (= P251), L129 (= L252), Y288 (= Y408), Y294 (= Y414), R328 (≠ T448), G372 (= G491), Y374 (= Y493)
2bt3A Agao in complex with ruthenium-c4-wire at 1.73 angstroms (see paper)
29% identity, 83% coverage: 122:747/752 of query aligns to 3:615/620 of 2bt3A
- active site: Y276 (= Y396), D290 (= D410), Y374 (= Y493), H423 (= H551), H425 (= H553), H584 (= H716)
- binding copper (ii) ion: H423 (= H551), H425 (= H553), H584 (= H716)
- binding bis[1h,1'h-2,2'-bipyridinato(2-)-kappa~2~n~1~,n~1'~]{3-[4-(1,10-dihydro-1,10-phenanthrolin-4-yl-kappa~2~n~1~,n~10~)butoxy]-n,n-dimethylanilinato(2-)}ruthenium: E94 (≠ L216), F97 (= F219), P128 (= P251), L129 (= L252), Y288 (= Y408), Y294 (= Y414), Q298 (≠ T418), Y299 (≠ L419), R328 (≠ T448), G372 (= G491), Y374 (= Y493)
Query Sequence
>BWI76_RS13080 FitnessBrowser__Koxy:BWI76_RS13080
MAILSPRKTALALAVALFCAWQSPAFAHGGEAHMVPMDKTLQDFGVDVQWDDYAQMFTLI
KDGAYVKVKPGAKTAIVNGKTLELQVPVVMKDGKAWVSDTFINDVFQSGLDQTFQVEKRP
HPLNSLSAAEISAAVAIVKAAADFKPNTRFTEISLREPDKKAVWDFALNGTPVNAPRTAD
VIMLDGKHVIEAVVDLQNKKVLSWTPIKDAHGMVLLDDFASVQNIINASSEFAEVLKKHG
IDDPSKVITTPLTVGYFDGKDGLKQDARLLKVVSYLDVGDGNYWAHPIENLVAVVDLEQK
KIIKIEEGPTIPVPMAARPYDGRDRVAPTVKPLEIIEPEGKNYTITGDMIHWRNWDFHLR
MNSRVGPILSTVTWNDNGKKRQVMYEGSLGGMIVPYGDPDVGWYFKAYLDSGDYGMGTLT
SPIVRGKDAPSNAVLLDETIADYTGTPTTIPRAIAIFERYAGPEYKHLEMGKPNVSTERR
ELVVRWISTVGNYDYIFDWVFHENGTIGIDAGATGIEAVKGVQAKTMHDPSAKEDTRYGT
LIDHNIVGTTHQHIYNFRLDLDVDGENNTLVAMDPEVKPNTAGGPRTSTMQINQYTIASE
QKAAQKFDPGTIRLLSNTTKENRMGNPVSYQIIPYAGGTHPVATGAKFAPDEWIYHRLSF
MDKQLWVTRYHPTERFPEGKYPNRSIHDTGLGQYAKDDESLDNHDDVVWITTGTTHVARA
EEWPIMPTEWAHALLKPWNFFDETPTLGEKKQ
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