Structure of PDB 2ctc Chain A

Receptor sequence
>2ctcA (length=307) Species: 9913 (Bos taurus) [Search protein sequence]
ARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVL
KFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTEDYGQDPSFTAIL
DSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAG
FGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQ
LLLYPYGYTTQSIPDKTELNQVAKSAVEALKSLYGTSYKYGSIITTIYQA
SGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTI
MEHTLNN
3D structure
PDB2ctc High-resolution structure of the complex between carboxypeptidase A and L-phenyl lactate.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) 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 HFA A H69 N144 R145 I243 Y248 A250 E270 H69 N144 R145 I243 Y248 A250 E270 MOAD: Ki=0.13mM
PDBbind-CN: -logKd/Ki=3.89,Ki=0.13mM
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:2ctc, PDBe:2ctc, PDBj:2ctc
PDBsum2ctc
PubMed15299490
UniProtP00730|CBPA1_BOVIN Carboxypeptidase A1 (Gene Name=CPA1)

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