Structure of PDB 1irj Chain D Binding Site BS03

Receptor Information
>1irj Chain D (length=82) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENK
NEKVIEHIMEDLDTNADKQLSFEEFIMLMARL
Ligand information
Ligand IDCPS
InChIInChI=1S/C32H58N2O7S/c1-21(8-11-29(38)33-14-6-15-34(4,5)16-7-17-42(39,40)41)24-9-10-25-30-26(20-28(37)32(24,25)3)31(2)13-12-23(35)18-22(31)19-27(30)36/h21-28,30,35-37H,6-20H2,1-5H3,(H-,33,38,39,40,41)/t21-,22+,23-,24-,25+,26+,27-,28+,30+,31+,32-/m1/s1
InChIKeyUMCMPZBLKLEWAF-BCTGSCMUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(CCC(=O)NCCC[N+](C)(C)CCCS(=O)(=O)[O-])C1CCC2C1(C(CC3C2C(CC4C3(CCC(C4)O)C)O)O)C
CACTVS 3.341C[C@H](CCC(=O)NCCC[N+](C)(C)CCC[S]([O-])(=O)=O)[C@H]1CC[C@H]2[C@@H]3[C@H](O)C[C@@H]4C[C@H](O)CC[C@]4(C)[C@H]3C[C@H](O)[C@]12C
OpenEye OEToolkits 1.5.0C[C@H](CCC(=O)NCCC[N+](C)(C)CCCS(=O)(=O)[O-])[C@H]1CC[C@@H]2[C@@]1([C@H](C[C@H]3[C@H]2[C@@H](C[C@H]4[C@@]3(CC[C@H](C4)O)C)O)O)C
CACTVS 3.341C[CH](CCC(=O)NCCC[N+](C)(C)CCC[S]([O-])(=O)=O)[CH]1CC[CH]2[CH]3[CH](O)C[CH]4C[CH](O)CC[C]4(C)[CH]3C[CH](O)[C]12C
ACDLabs 10.04[O-]S(=O)(=O)CCC[N+](C)(C)CCCNC(=O)CCC(C3CCC2C1C(O)CC4CC(O)CCC4(C)C1CC(O)C23C)C
FormulaC32 H58 N2 O7 S
Name3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE;
CHAPS
ChEMBLCHEMBL450950
DrugBank
ZINC
PDB chain1irj Chain D Residue 289 [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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PDB1irj The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent regulator protein in inflammatory process.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		F48 E52 H61 D65 L86
Binding residue
(residue number reindexed from 1)		F44 E48 H57 D61 L82
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008017 microtubule binding
GO:0008270 zinc ion binding
GO:0016209 antioxidant activity
GO:0035662 Toll-like receptor 4 binding
GO:0046872 metal ion binding
GO:0048306 calcium-dependent protein binding
GO:0050544 arachidonate binding
GO:0050786 RAGE receptor binding
Biological Process
GO:0002523 leukocyte migration involved in inflammatory response
GO:0002544 chronic inflammatory response
GO:0006914 autophagy
GO:0006915 apoptotic process
GO:0006919 activation of cysteine-type endopeptidase activity involved in apoptotic process
GO:0006935 chemotaxis
GO:0006954 inflammatory response
GO:0007267 cell-cell signaling
GO:0010976 positive regulation of neuron projection development
GO:0014002 astrocyte development
GO:0030307 positive regulation of cell growth
GO:0030593 neutrophil chemotaxis
GO:0032119 sequestering of zinc ion
GO:0032496 response to lipopolysaccharide
GO:0034121 regulation of toll-like receptor signaling pathway
GO:0035425 autocrine signaling
GO:0035606 peptidyl-cysteine S-trans-nitrosylation
GO:0035821 modulation of process of another organism
GO:0042742 defense response to bacterium
GO:0043542 endothelial cell migration
GO:0045087 innate immune response
GO:0045113 regulation of integrin biosynthetic process
GO:0050729 positive regulation of inflammatory response
GO:0050832 defense response to fungus
GO:0051092 positive regulation of NF-kappaB transcription factor activity
GO:0051493 regulation of cytoskeleton organization
GO:0060264 regulation of respiratory burst involved in inflammatory response
GO:0061844 antimicrobial humoral immune response mediated by antimicrobial peptide
GO:0070488 neutrophil aggregation
GO:0098869 cellular oxidant detoxification
GO:2001244 positive regulation of intrinsic apoptotic signaling pathway
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005856 cytoskeleton
GO:0005886 plasma membrane
GO:0034774 secretory granule lumen
GO:0062023 collagen-containing extracellular matrix
GO:0070062 extracellular exosome
GO:1990660 calprotectin complex
GO:1990662 S100A9 complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1irj, PDBe:1irj, PDBj:1irj
PDBsum1irj
PubMed11851337
UniProtP06702|S10A9_HUMAN Protein S100-A9 (Gene Name=S100A9)

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