Structure of PDB 1pq3 Chain E

Receptor sequence
>1pq3E (length=306) Species: 9606 (Homo sapiens) [Search protein sequence]
HSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSSLGCHLKDFGDLSF
TPVPKDDLYNNLIVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDHSLA
IGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQD
KVPQLPGFSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDID
RLGIQKVMERTFDLLIGKRQRPIHLSFDIDAFDPTLAPATGTPVVGGLTY
REGMYIAEEIHNTGLLSALDLVEVNPQLATSEEEAKTTANLAVDVIASSF
GQTREG
3D structure
PDB1pq3 Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal
ChainE
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) 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.
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 MN E H120 D143 D147 D251 H97 D120 D124 D228
BS02 MN E D143 H145 D251 D253 D120 H122 D228 D230
BS03 S2C E H145 D147 S156 H160 D202 D251 E296 H122 D124 S133 H137 D179 D228 E273
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
View graph for
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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