Structure of PDB 4hxq Chain B Binding Site BS01

Receptor Information
>4hxq Chain B (length=314) 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
GLAREGNHKPIDYL
Ligand information
Ligand IDX8A
InChIInChI=1S/C14H30BN2O5/c1-16-14(13(18)19,7-3-4-9-15(20,21)22)8-12-17-10-5-2-6-11-17/h16,20-22H,2-12H2,1H3,(H,18,19)/q-1/t14-/m1/s1
InChIKeyXUSDRKPOXSYXRQ-CQSZACIVSA-N
SMILES
SoftwareSMILES
CACTVS 3.370CN[C@](CCCC[B-](O)(O)O)(CCN1CCCCC1)C(O)=O
ACDLabs 12.01O=C(O)C(NC)(CCN1CCCCC1)CCCC[B-](O)(O)O
CACTVS 3.370CN[C](CCCC[B-](O)(O)O)(CCN1CCCCC1)C(O)=O
OpenEye OEToolkits 1.7.6[B-](CCCC[C@@](CCN1CCCCC1)(C(=O)O)NC)(O)(O)O
OpenEye OEToolkits 1.7.6[B-](CCCCC(CCN1CCCCC1)(C(=O)O)NC)(O)(O)O
FormulaC14 H30 B N2 O5
Name[(5R)-5-carboxy-5-(methylamino)-7-(piperidin-1-yl)heptyl](trihydroxy)borate(1-)
ChEMBL
DrugBank
ZINCZINC000206367263
PDB chain4hxq Chain B Residue 401 [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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PDB4hxq Discovery of (R)-2-Amino-6-borono-2-(2-(piperidin-1-yl)ethyl)hexanoic Acid and Congeners As Highly Potent Inhibitors of Human Arginases I and II for Treatment of Myocardial Reperfusion Injury.
Resolution1.45 Å
Binding residue
(original residue number in PDB)		D124 H126 D128 S137 H141 D183 D232
Binding residue
(residue number reindexed from 1)		D120 H122 D124 S133 H137 D179 D228
Annotation score1
Binding affinityMOAD: ic50=60nM
PDBbind-CN: -logKd/Ki=7.22,IC50=60nM
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:4hxq, PDBe:4hxq, PDBj:4hxq
PDBsum4hxq
PubMed23472952
UniProtP05089|ARGI1_HUMAN Arginase-1 (Gene Name=ARG1)

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