Structure of PDB 3skk Chain A

Receptor sequence
>3skkA (length=314) Species: 9606 (Homo sapiens) [Search protein sequence]
RTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPF
ADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAI
GSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGK
IPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDR
LGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTYR
EGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACFG
LAREGNHKPIDYLN
3D structure
PDB3skk Binding of alpha , alpha-disubstituted amino acids to arginase suggests new avenues for inhibitor design.
ChainA
Resolution1.701 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 D124 H126 D232 D234 D119 H121 D227 D229
BS02 MN A H101 D124 D128 D232 H96 D119 D123 D227
BS03 4U7 A D124 H126 D128 S137 H141 D183 D232 D119 H121 D123 S132 H136 D178 D227 PDBbind-CN: -logKd/Ki=4.47,Kd=34uM
Gene Ontology
Molecular Function
GO:0004053 arginase activity
GO:0005515 protein binding
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:0046872 metal ion binding
Biological Process
GO:0000050 urea cycle
GO:0002250 adaptive immune response
GO:0006525 arginine metabolic process
GO:0006527 arginine catabolic process
GO:0009624 response to nematode
GO:0019547 arginine catabolic process to ornithine
GO:0042130 negative regulation of T cell proliferation
GO:0042832 defense response to protozoan
GO:0045087 innate immune response
GO:0046007 negative regulation of activated T cell proliferation
GO:0060336 negative regulation of type II interferon-mediated signaling pathway
GO:0070965 positive regulation of neutrophil mediated killing of fungus
GO:2000552 negative regulation of T-helper 2 cell cytokine production
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0035578 azurophil granule lumen
GO:0035580 specific granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3skk, PDBe:3skk, PDBj:3skk
PDBsum3skk
PubMed21728378
UniProtP05089|ARGI1_HUMAN Arginase-1 (Gene Name=ARG1)

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