Structure of PDB 2pcu Chain A

Receptor sequence
>2pcuA (length=305) Species: 9606 (Homo sapiens) [Search protein sequence]
NNFNYGAYHSLEAIYHEMDNIAADFPDLARRVKIGHSFENRPMYVLKFST
GKGVRRPAVWLNAGIHSREWISQATAIWTARKIVSDYQRDPAITSILEKM
DIFLLPVANPDGYVYTQTQNRLWRKTRSRNPGSSCIGADPNRNWNASFAG
KGASDNPCSEVYHGPHANSEVEVKSVVDFIQKHGNFKGFIDLHSYSQLLM
YPYGYSVKKAPDAEELDKVARLAAKALASVSGTEYQVGPTCTTVYPASGS
SIDWAYDNGIKFAFTFELRDTGTYGFLLPANQIIPTAEETWLGLKTIMEH
VRDNL
3D structure
PDB2pcu Caught after the Act: a human A-type metallocarboxypeptidase in a product complex with a cleaved hexapeptide.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H69 E72 R127 H196 E270
Catalytic site (residue number reindexed from 1) H66 E69 R124 H193 E267
Enzyme Commision number 3.4.17.-
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 peptide A H69 R71 E72 R127 E163 H196 S197 Y198 V247 Y248 E270 H66 R68 E69 R124 E160 H193 S194 Y195 V244 Y245 E267
BS02 ZN A H69 E72 H196 H66 E69 H193
BS03 ASP A H69 R127 N144 R145 H196 Y248 T268 E270 H66 R124 N141 R142 H193 Y245 T265 E267
Gene Ontology
Molecular Function
GO:0004181 metallocarboxypeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:2pcu, PDBe:2pcu, PDBj:2pcu
PDBsum2pcu
PubMed17506531
UniProtQ9UI42|CBPA4_HUMAN Carboxypeptidase A4 (Gene Name=CPA4)

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