Structure of PDB 6cpa Chain A

Receptor sequence
>6cpaA (length=307) Species: 9913 (Bos taurus) [Search protein sequence]
ARSTNTFNYATYHTLDEIYDFMDLLVAQHPELVSKLQIGRSYEGRPIYVL
KFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTENYGQNPSFTAIL
DSMDIFLEIVTNPNGFAFTHSENRLWRKTRSVTSSSLCVGVDANRNWDAG
FGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKNHGNFKAFLSIHSYSQ
LLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKYGSIITTIYQA
SGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTI
MEHTVNN
3D structure
PDB6cpa Crystal structure of the complex of carboxypeptidase A with a strongly bound phosphonate in a new crystalline form: comparison with structures of other complexes.
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 ZAF A H69 E72 R127 N144 R145 E163 H196 I243 Y248 A250 E270 H69 E72 R127 N144 R145 E163 H196 I243 Y248 A250 E270 MOAD: Ki=3pM
PDBbind-CN: -logKd/Ki=11.52,Ki=3pM
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:6cpa, PDBe:6cpa, PDBj:6cpa
PDBsum6cpa
PubMed2386784
UniProtP00730|CBPA1_BOVIN Carboxypeptidase A1 (Gene Name=CPA1)

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