Structure of PDB 3mfw Chain A Binding Site BS01

Receptor Information
>3mfw Chain A (length=315) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLP
FADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLA
IGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKG
KIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVD
RLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTY
REGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACF
GLAREGNHKPIDYLN
Ligand information
Ligand IDB3U
InChIInChI=1S/C6H10N4O2/c7-4(5(11)12)1-3-2-9-6(8)10-3/h2,4H,1,7H2,(H,11,12)(H3,8,9,10)/t4-/m0/s1
InChIKeyUYEGXSNFZXWSDV-BYPYZUCNSA-N
SMILES
SoftwareSMILES
CACTVS 3.370N[CH](Cc1[nH]c(N)nc1)C(O)=O
ACDLabs 12.01O=C(O)C(N)Cc1cnc(N)n1
OpenEye OEToolkits 1.7.0c1c([nH]c(n1)N)CC(C(=O)O)N
OpenEye OEToolkits 1.7.0c1c([nH]c(n1)N)C[C@@H](C(=O)O)N
CACTVS 3.370N[C@@H](Cc1[nH]c(N)nc1)C(O)=O
FormulaC6 H10 N4 O2
Name2-amino-L-histidine
ChEMBLCHEMBL1099167
DrugBank
ZINCZINC000026286704
PDB chain3mfw Chain A Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3mfw 2-aminoimidazole amino acids as inhibitors of the binuclear manganese metalloenzyme human arginase I.
Resolution1.47 Å
Binding residue
(original residue number in PDB)		H126 D128 N130 S137 H141 G142 D183 T246
Binding residue
(residue number reindexed from 1)		H122 D124 N126 S133 H137 G138 D179 T242
Annotation score1
Binding affinityMOAD: Ki=300uM
PDBbind-CN: -logKd/Ki=3.52,Ki=300uM
BindingDB: Ki=300000nM
Enzymatic activity
Catalytic site (original residue number in PDB) H101 D124 H126 D128 H141 D232 D234 E277
Catalytic site (residue number reindexed from 1) H97 D120 H122 D124 H137 D228 D230 E273
Enzyme Commision number 3.5.3.1: arginase.
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:3mfw, PDBe:3mfw, PDBj:3mfw
PDBsum3mfw
PubMed20441173
UniProtP05089|ARGI1_HUMAN Arginase-1 (Gene Name=ARG1)

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