Structure of PDB 3fvl Chain A

Receptor sequence
>3fvlA (length=307) Species: 9913 (Bos taurus) [Search protein sequence]
ARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVL
KFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTEDYGQDPSFTAIL
DSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAG
FGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQ
LLLYPYGYTTQSIPDKTELNQVAKSAVEALKSLYGTSYKYGSIITTIYQA
SGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTI
MEHTVNN
3D structure
PDB3fvl Optical 2-benzyl-5-hydroxy4oxopentanoic acids against carboxypeptidase A: Synthesis, kinetic evaluation and X-ray crystallographic study
ChainA
Resolution1.85 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 BHK A E72 N144 R145 H196 Y248 A250 G253 E270 E72 N144 R145 H196 Y248 A250 G253 E270 PDBbind-CN: -logKd/Ki=6.07,Ki=0.86uM
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:3fvl, PDBe:3fvl, PDBj:3fvl
PDBsum3fvl
PubMed
UniProtP00730|CBPA1_BOVIN Carboxypeptidase A1 (Gene Name=CPA1)

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