Structure of PDB 2rfh Chain A

Receptor sequence
>2rfhA (length=307) Species: 9913 (Bos taurus) [Search protein sequence]
ARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVL
KFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTEDYGQDPSFTAIL
DSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAG
FGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQ
LLLYPYGYTTQSIPDKTELNQVAKSAVAALKSLYGTSYKYGSIITTIYQA
SGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTI
MEHTVNN
3D structure
PDB2rfh Nitro as a novel zinc-binding group in the inhibition of carboxypeptidase A
ChainA
Resolution1.7 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 23N A H69 R127 N144 R145 H196 I243 A250 E270 H69 R127 N144 R145 H196 I243 A250 E270 MOAD: Ki=0.15uM
PDBbind-CN: -logKd/Ki=6.82,Ki=0.15uM
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:2rfh, PDBe:2rfh, PDBj:2rfh
PDBsum2rfh
PubMed18289863
UniProtP00730|CBPA1_BOVIN Carboxypeptidase A1 (Gene Name=CPA1)

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