Structure of PDB 1d3v Chain A

Receptor sequence

>1d3vA (length=308) Species: 10116 (Rattus norvegicus) [Search protein sequence]

KPIEIIGAPFSKGQPRGGVEKGPAALRKAGLVEKLKETEYNVRDHGDLAF
VDVPNDSPFQIVKNPRSVGKANEQLAAVVAETQKNGTISVVLGGDHSMAI
GSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGK
FPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDK
LGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYR
EGLYITEEIYKTGLLSGLDIMEVNPTLGKTPEEVTRTVNTAVALTLSCFG
TKREGNHK

3D structure

PDB

1d3v Arginase-boronic acid complex highlights a physiological role in erectile function.

Chain

Resolution

1.7 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	H101 D124 H126 D128 H141 D232 D234 E277
Catalytic site (residue number reindexed from 1)	H96 D119 H121 D123 H136 D227 D229 E272
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	H101 D124 D128 D232	H96 D119 D123 D227
BS02	MN	A	D124 H126 D232 D234	D119 H121 D227 D229
BS03	ABH	A	H101 D124 H126 D128 N130 S137 H141 D232	H96 D119 H121 D123 N125 S132 H136 D227	MOAD: Kd=0.11uM PDBbind-CN: -logKd/Ki=6.96,Kd=0.11uM

Gene Ontology

	Molecular Function
GO:0004053	arginase activity
GO:0016787	hydrolase activity
GO:0016813	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0030145	manganese ion binding
GO:0042802	identical protein binding
GO:0046872	metal ion binding

	Biological Process
GO:0000050	urea cycle
GO:0001889	liver development
GO:0001938	positive regulation of endothelial cell proliferation
GO:0002250	adaptive immune response
GO:0006525	arginine metabolic process
GO:0007565	female pregnancy
GO:0009410	response to xenobiotic stimulus
GO:0009635	response to herbicide
GO:0010042	response to manganese ion
GO:0010043	response to zinc ion
GO:0010269	response to selenium ion
GO:0014075	response to amine
GO:0019547	arginine catabolic process to ornithine
GO:0030324	lung development
GO:0032496	response to lipopolysaccharide
GO:0032964	collagen biosynthetic process
GO:0033189	response to vitamin A
GO:0033197	response to vitamin E
GO:0042130	negative regulation of T cell proliferation
GO:0042832	defense response to protozoan
GO:0043200	response to amino acid
GO:0043434	response to peptide hormone
GO:0045087	innate immune response
GO:0046007	negative regulation of activated T cell proliferation
GO:0046686	response to cadmium ion
GO:0048545	response to steroid hormone
GO:0048678	response to axon injury
GO:0051597	response to methylmercury
GO:0060056	mammary gland involution
GO:0060135	maternal process involved in female pregnancy
GO:0060336	negative regulation of type II interferon-mediated signaling pathway
GO:0070301	cellular response to hydrogen peroxide
GO:0070965	positive regulation of neutrophil mediated killing of fungus
GO:0071222	cellular response to lipopolysaccharide
GO:0071353	cellular response to interleukin-4
GO:0071377	cellular response to glucagon stimulus
GO:0071549	cellular response to dexamethasone stimulus
GO:0071560	cellular response to transforming growth factor beta stimulus
GO:1905541	regulation of L-arginine import across plasma membrane
GO:2000552	negative regulation of T-helper 2 cell cytokine production

	Cellular Component
GO:0005615	extracellular space
GO:0005737	cytoplasm
GO:0005741	mitochondrial outer membrane
GO:0005829	cytosol
GO:0043025	neuronal cell body

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:1d3v, PDBe:1d3v, PDBj:1d3v
PDBsum	1d3v
PubMed	10542097
UniProt	P07824\|ARGI1_RAT Arginase-1 (Gene Name=Arg1)

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