Structure of PDB 2pnc Chain A Binding Site BS01

Receptor Information
>2pnc Chain A (length=623) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QLFADLSREELTTVMSFLTQQLGPDLVDAAQARPSDNCVFSVELQLPPKA
AALAHLDRGSPPPAREALAIVFFGGQPQPNVTELVVGPLPQPSYMRDVTV
ERHGGPLPYYRRPVLLREYLDIDQMIFNRELPQAAGVLHHCCSYKQGGQK
LLTMNSAPRGVQSGDRSTWFGIYYNITKGGPYLHPVGLELLVDHKALDPA
DWTVQKVFFQGRYYENLAQLEEQFEAGQVNVVVIPDRFSVQGNRVASSLW
TFSFGLGAFSGPRVFDVRFQGERLAYEISLQEAGAVYGGNTPAAMLTRYM
DSGFGMGYFATPLIRGVDCPYLATYMDWHFVVESQTPKTLHDAFCVFEQN
KGLPLRRGGVAQTVLVFRSVSTMLNYDYVWDMVFYPNGAIEVKLHATGYI
SSAFLFGAARRYGNQVGEHTLGPVHTHSAHYKVDLDVGGLENWVWAEDMA
FVPTAIPWSPEHQIQRLQVTRKQLETEEQAAFPLGGASPRYLYLASKQSN
KWGHPRGYRIQTVSFAGGPMPQNSPMERAFSWGRYQLAITQRKETEPSSS
SVFNQNDPWTPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTV
TVGNGVGFFLRPYNFFDQEPSMD
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 chain2pnc Chain A Residue 804 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2pnc Multiple binding sites for substrates and modulators of semicarbazide-sensitive amine oxidases: kinetic consequences
Resolution2.4 Å
Binding residue
(original residue number in PDB)		A470 H519 H521 H683
Binding residue
(residue number reindexed from 1)		A376 H425 H427 H589
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y371 D385 Y470 H519 H521 H683
Catalytic site (residue number reindexed from 1) Y287 D301 Y376 H425 H427 H589
Enzyme Commision number 1.4.3.21: primary-amine oxidase.
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0008131 primary methylamine oxidase activity
GO:0016491 oxidoreductase activity
GO:0016641 oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
GO:0046872 metal ion binding
GO:0048038 quinone binding
GO:0052595 aliphatic amine oxidase activity
Biological Process
GO:0009308 amine metabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0005576 extracellular region
GO:0005769 early endosome
GO:0005783 endoplasmic reticulum
GO:0005794 Golgi apparatus
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2pnc, PDBe:2pnc, PDBj:2pnc
PDBsum2pnc
PubMed17989349
UniProtQ29437|AOCX_BOVIN Primary amine oxidase, liver isozyme

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