Structure of PDB 2w0q Chain B Binding Site BS05

Receptor Information
>2w0q Chain B (length=720) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPL
ALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIK
QAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVI
MLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEF
AAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGN
YWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKP
MQIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRK
VMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPSN
AVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERREL
VVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETA
KDDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTA
GGPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQI
IPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYP
NRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVH
TLLKPWNFFDETPTLGALKK
Ligand information
Ligand IDXE
InChIInChI=1S/Xe
InChIKeyFHNFHKCVQCLJFQ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Xe]
FormulaXe
NameXENON
ChEMBLCHEMBL1236802
DrugBankDB13453
ZINC
PDB chain2w0q Chain B Residue 902 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2w0q Structure of a Xenon Derivative of Escherichia Coli Copper Amine Oxidase: Confirmation of the Proposed Oxygen-Entry Pathway.
Resolution2.48 Å
Binding residue
(original residue number in PDB)		V187 L188 L189 Y387
Binding residue
(residue number reindexed from 1)		V182 L183 L184 Y382
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y369 D383 Y466 H524 H526 H689
Catalytic site (residue number reindexed from 1) Y364 D378 Y461 H519 H521 H684
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:2w0q, PDBe:2w0q, PDBj:2w0q
PDBsum2w0q
PubMed19052360
UniProtP46883|AMO_ECOLI Primary amine oxidase (Gene Name=tynA)

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