Structure of PDB 1cg2 Chain C Binding Site BS01

Receptor Information
>1cg2 Chain C (length=389) Species: 312 (Pseudomonas sp. RS-16) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELK
NLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYLKGILAKA
PFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDE
EKGSFGSRDLIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG
KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNWTIAKAGNVSN
IIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRGRP
AFNAGEGGKKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGKPVIE
SLGLPGFGYHSDKAEYVDISAIPRRLYMAARLIMDLGAG
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1cg2 Chain C Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1cg2 Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		D141 E176 H385
Binding residue
(residue number reindexed from 1)		D116 E151 H360
Annotation score1
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.
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

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

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