Structure of PDB 7klm Chain D Binding Site BS03

Receptor Information
>7klm Chain D (length=317) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGD
LPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHS
LAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKEL
KGKIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTE
VDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGL
TYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLA
CFGLAREGNHKPIDYLN
Ligand information
Ligand ID0IZ
InChIInChI=1S/C13H27BN3O6/c1-7(2)10(15)12(18)17-9-6-16-11(13(19)20)8(9)4-3-5-14(21,22)23/h7-11,16,21-23H,3-6,15H2,1-2H3,(H,17,18)(H,19,20)/q-1/t8-,9+,10+,11+/m1/s1
InChIKeyBIHQJUDSCKNIPN-RCWTZXSCSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7[B-](CCCC1C(CNC1C(=O)O)NC(=O)C(C(C)C)N)(O)(O)O
CACTVS 3.385CC(C)[C@H](N)C(=O)N[C@H]1CN[C@@H]([C@@H]1CCC[B-](O)(O)O)C(O)=O
ACDLabs 12.01O=C(NC1CNC(C1CCC[B-](O)(O)O)C(=O)O)C(N)C(C)C
OpenEye OEToolkits 2.0.7[B-](CCC[C@@H]1[C@H](CN[C@@H]1C(=O)O)NC(=O)[C@H](C(C)C)N)(O)(O)O
CACTVS 3.385CC(C)[CH](N)C(=O)N[CH]1CN[CH]([CH]1CCC[B-](O)(O)O)C(O)=O
FormulaC13 H27 B N3 O6
Name3-[(2~{S},3~{R},4~{R})-4-[[(2~{S})-2-azanyl-3-methyl-butanoyl]amino]-2-carboxy-pyrrolidin-3-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boron
ChEMBL
DrugBank
ZINC
PDB chain7klm Chain D Residue 1003 [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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PDB7klm Structure-Based Discovery of Proline-Derived Arginase Inhibitors with Improved Oral Bioavailability for Immuno-Oncology.
Resolution2.27 Å
Binding residue
(original residue number in PDB)		D124 H126 D128 S137 H141 G142 D181 D183 D232 D234 T246 E277
Binding residue
(residue number reindexed from 1)		D122 H124 D126 S135 H139 G140 D179 D181 D230 D232 T244 E275
Annotation score1
Enzymatic activity
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:7klm, PDBe:7klm, PDBj:7klm
PDBsum7klm
PubMed34527178
UniProtP05089|ARGI1_HUMAN Arginase-1 (Gene Name=ARG1)

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