Structure of PDB 1cbx Chain A

Receptor sequence
>1cbxA (length=307) Species: 9913 (Bos taurus) [Search protein sequence]
ARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVL
KFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTENYGQNPSFTAIL
DSMDIFLEIVTNPNGFAFTHSENRLWRKTRSVTSSSLCVGVDANRNWDAG
FGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKNHGNFKAFLSIHSYSQ
LLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKYGSIITTIYQA
SGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTI
MEHTVNN
3D structure
PDB1cbx Crystal structure of the complex between carboxypeptidase A and the biproduct analog inhibitor L-benzylsuccinate at 2.0 A resolution.
ChainA
Resolution2.0 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) H69 E72 R127 H196 E270
Enzyme Commision number 3.4.17.1: carboxypeptidase A.
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 ZN A H69 E72 H196 H69 E72 H196
BS02 BZS A H69 R127 N144 R145 H196 I243 Y248 E270 H69 R127 N144 R145 H196 I243 Y248 E270 MOAD: Ki=0.45uM
PDBbind-CN: -logKd/Ki=6.35,Ki=0.45uM
BindingDB: Ki=500nM
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:1cbx, PDBe:1cbx, PDBj:1cbx
PDBsum1cbx
PubMed1738164
UniProtP00730|CBPA1_BOVIN Carboxypeptidase A1 (Gene Name=CPA1)

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