Structure of PDB 1pq3 Chain C Binding Site BS02

Receptor Information
>1pq3 Chain C (length=306) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSSLGCHLKDFGDLSF
TPVPKDDLYNNLIVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDHSLA
IGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQD
KVPQLPGFSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDID
RLGIQKVMERTFDLLIGKRQRPIHLSFDIDAFDPTLAPATGTPVVGGLTY
REGMYIAEEIHNTGLLSALDLVEVNPQLATSEEEAKTTANLAVDVIASSF
GQTREG
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain1pq3 Chain C Residue 505 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1pq3 Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal
Resolution2.7 Å
Binding residue
(original residue number in PDB)		H120 D143 D147 D251
Binding residue
(residue number reindexed from 1)		H97 D120 D124 D228
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H120 D143 H145 D147 H160 D251 D253 E296
Catalytic site (residue number reindexed from 1) H97 D120 H122 D124 H137 D228 D230 E273
Enzyme Commision number 3.5.3.1: arginase.
Gene Ontology
Molecular Function
GO:0004053 arginase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0046872 metal ion binding
Biological Process
GO:0006525 arginine metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1pq3, PDBe:1pq3, PDBj:1pq3
PDBsum1pq3
PubMed12859189
UniProtP78540|ARGI2_HUMAN Arginase-2, mitochondrial (Gene Name=ARG2)

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