Structure of PDB 1cg2 Chain C

Receptor sequence
>1cg2C (length=389) Species: 312 (Pseudomonas sp. RS-16) [Search protein sequence]
QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELK
NLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYLKGILAKA
PFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDE
EKGSFGSRDLIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG
KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNWTIAKAGNVSN
IIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRGRP
AFNAGEGGKKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGKPVIE
SLGLPGFGYHSDKAEYVDISAIPRRLYMAARLIMDLGAG
3D structure
PDB1cg2 Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy.
ChainC
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H112 D141 E175 E176 E200 H385
Catalytic site (residue number reindexed from 1) H87 D116 E150 E151 E175 H360
Enzyme Commision number 3.4.17.11: glutamate carboxypeptidase.
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 C D141 E176 H385 D116 E151 H360
BS02 ZN C H112 D141 E200 H87 D116 E175
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0008237 metallopeptidase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1cg2, PDBe:1cg2, PDBj:1cg2
PDBsum1cg2
PubMed9083113
UniProtP06621|CBPG_PSES6 Carboxypeptidase G2 (Gene Name=cpg2)

[Back to BioLiP]