Structure of PDB 4ie3 Chain A

Receptor sequence
>4ie3A (length=306) Species: 9606 (Homo sapiens) [Search protein sequence]
HSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSSLGCHLKDFGDLSF
TPVPKDDLYNNLIVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDHSLA
IGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQD
KVPQLPGFSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDID
RLGIQKVMERTFDLLIGKRQRPIHLSFDIDAFDPTLAPATGTPVVGGLTY
REGMYIAEEIHNTGLLSALDLVEVNPQLATSEEEAKTTANLAVDVIASSF
GQTREG
3D structure
PDB4ie3 2-Substituted-2-amino-6-boronohexanoic acids as arginase inhibitors.
ChainA
Resolution2.3522 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 A H120 D143 D147 D251 H97 D120 D124 D228
BS02 MN A D143 H145 D251 D253 D120 H122 D228 D230
BS03 1EE A D143 H145 D147 N149 S156 H160 D202 D251 D120 H122 D124 N126 S133 H137 D179 D228 MOAD: ic50=980nM
PDBbind-CN: -logKd/Ki=6.01,IC50=980nM
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:4ie3, PDBe:4ie3, PDBj:4ie3
PDBsum4ie3
PubMed23453840
UniProtP78540|ARGI2_HUMAN Arginase-2, mitochondrial (Gene Name=ARG2)

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