Structure of PDB 1oac Chain A

Receptor sequence
>1oacA (length=720) Species: 562 (Escherichia coli) [Search protein sequence]
AHMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQP
LALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEI
KQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADV
IMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEE
FAAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDG
NYWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVK
PMQIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKR
KVMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPS
NAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERRE
LVVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDET
AKDDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNT
AGGPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQ
IIPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKY
PNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWV
HTLLKPWNFFDETPTLGALK
3D structure
PDB1oac Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y369 D383 Y466 H524 H526 H689
Catalytic site (residue number reindexed from 1) Y365 D379 Y462 H520 H522 H685
Enzyme Commision number 1.4.3.21: primary-amine oxidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CU A A466 H524 H526 H689 A462 H520 H522 H685
BS02 CA A D533 L534 D535 D678 A679 D529 L530 D531 D674 A675
BS03 CA A E573 Y667 D670 E672 E569 Y663 D666 E668
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0005509 calcium ion binding
GO:0008131 primary methylamine oxidase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0048038 quinone binding
GO:0052595 aliphatic amine oxidase activity
Biological Process
GO:0006559 L-phenylalanine catabolic process
GO:0009308 amine metabolic process
GO:0019607 phenylethylamine catabolic process
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1oac, PDBe:1oac, PDBj:1oac
PDBsum1oac
PubMed8591028
UniProtP46883|AMO_ECOLI Primary amine oxidase (Gene Name=tynA)

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