Structure of PDB 4rla Chain B

Receptor sequence
>4rlaB (length=314) Species: 10116 (Rattus norvegicus) [Search protein sequence]
KPIEIIGAPFSKGQPRGGVEKGPAALRKAGLVEKLKETEYNVRDHGDLAF
VDVPNDSPFQIVKNPRSVGKANEQLAAVVAETQKNGTISVVLGGDNSMAI
GSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGK
FPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDK
LGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYR
EGLYITEEIYKTGLLSGLDIMEVNPTLGKTPEEVTRTVNTAVALTLSCFG
TKREGNHKPETDYL
3D structure
PDB4rla Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function.
ChainB
Resolution2.94 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N101 D124 H126 D128 H141 D232 D234 E277
Catalytic site (residue number reindexed from 1) N96 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 B D124 H126 D232 D234 D119 H121 D227 D229
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4rla, PDBe:4rla, PDBj:4rla
PDBsum4rla
PubMed9265637
UniProtP07824|ARGI1_RAT Arginase-1 (Gene Name=Arg1)

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