Structure of PDB 2pnc Chain A

Receptor sequence
>2pncA (length=623) Species: 9913 (Bos taurus) [Search protein sequence]
QLFADLSREELTTVMSFLTQQLGPDLVDAAQARPSDNCVFSVELQLPPKA
AALAHLDRGSPPPAREALAIVFFGGQPQPNVTELVVGPLPQPSYMRDVTV
ERHGGPLPYYRRPVLLREYLDIDQMIFNRELPQAAGVLHHCCSYKQGGQK
LLTMNSAPRGVQSGDRSTWFGIYYNITKGGPYLHPVGLELLVDHKALDPA
DWTVQKVFFQGRYYENLAQLEEQFEAGQVNVVVIPDRFSVQGNRVASSLW
TFSFGLGAFSGPRVFDVRFQGERLAYEISLQEAGAVYGGNTPAAMLTRYM
DSGFGMGYFATPLIRGVDCPYLATYMDWHFVVESQTPKTLHDAFCVFEQN
KGLPLRRGGVAQTVLVFRSVSTMLNYDYVWDMVFYPNGAIEVKLHATGYI
SSAFLFGAARRYGNQVGEHTLGPVHTHSAHYKVDLDVGGLENWVWAEDMA
FVPTAIPWSPEHQIQRLQVTRKQLETEEQAAFPLGGASPRYLYLASKQSN
KWGHPRGYRIQTVSFAGGPMPQNSPMERAFSWGRYQLAITQRKETEPSSS
SVFNQNDPWTPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTV
TVGNGVGFFLRPYNFFDQEPSMD
3D structure
PDB2pnc Multiple binding sites for substrates and modulators of semicarbazide-sensitive amine oxidases: kinetic consequences
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 A470 H519 H521 H683 A376 H425 H427 H589
BS02 CA A L529 D530 D672 L673 L435 D436 D578 L579
BS03 CA A E571 K637 E640 F662 N664 E666 E477 K543 E546 F568 N570 E572
BS04 CLU A Y383 D385 M467 A470 D471 Y472 H521 Y299 D301 M373 A376 D377 Y378 H427 MOAD: Ki=466uM
PDBbind-CN: -logKd/Ki=3.33,Ki=466uM
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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