Structure of PDB 1lvn Chain A Binding Site BS01

Receptor Information
>1lvn Chain A (length=718) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPLA
LQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIKQ
AVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVIM
LDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFA
AAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNY
WAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPM
QIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRKV
MYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPSNA
VLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERRELV
VRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAK
DDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAG
GPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQII
PYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYPN
RSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVHT
LLKPWNFFDETPTLGALK
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 chain1lvn 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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PDB1lvn Medical implications from the crystal structure of a copper-containing amine oxidase complexed with the antidepressant drug tranylcypromine.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		H524 H526 H689
Binding residue
(residue number reindexed from 1)		H518 H520 H683
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y369 D383 H524 H526 H689
Catalytic site (residue number reindexed from 1) Y363 D377 H517 H519 H682
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:1lvn, PDBe:1lvn, PDBj:1lvn
PDBsum1lvn
PubMed15498552
UniProtP46883|AMO_ECOLI Primary amine oxidase (Gene Name=tynA)

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