Structure of PDB 1hqx Chain A Binding Site BS02
Receptor Information
>1hqx Chain A (length=314) Species:
10116
(Rattus norvegicus) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
KPIEIIGAPFSKGQPRGGVEKGPAALRKAGLVEKLKETEYNVRDHGDLAF
VDVPNDSPFQIVKNPRSVGKANEQLAAVVAETQKNGTISVVLGGDHSMAI
GSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGK
FPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDK
LGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYR
EGLYITEEIYKTGLLSGLDIMEVNPTLGKTPEEVTRTVNTAVALTLSCFG
TKKEGNHKPETDYL
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
1hqx Chain A Residue 501 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
1hqx
Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid.
Resolution
3.0 Å
Binding residue
(original residue number in PDB)
D124 H126 D128 D232 D234
Binding residue
(residue number reindexed from 1)
D119 H121 D123 D227 D229
Annotation score
1
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.
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:1hqx
,
PDBe:1hqx
,
PDBj:1hqx
PDBsum
1hqx
PubMed
11278703
UniProt
P07824
|ARGI1_RAT Arginase-1 (Gene Name=Arg1)
[
Back to BioLiP
]