Structure of PDB 1oac Chain A Binding Site BS01

Receptor Information
>1oac Chain A (length=720) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AHMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQP
LALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEI
KQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADV
IMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEE
FAAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDG
NYWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVK
PMQIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKR
KVMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPS
NAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERRE
LVVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDET
AKDDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNT
AGGPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQ
IIPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKY
PNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWV
HTLLKPWNFFDETPTLGALK
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain1oac Chain A Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1oac Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		A466 H524 H526 H689
Binding residue
(residue number reindexed from 1)		A462 H520 H522 H685
Annotation score1
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.
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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