Structure of PDB 1isi Chain B Binding Site BS02

Receptor Information
>1isi Chain B (length=250) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
WRAEGTSAHLRDIFLGRCAEYRALLSPEQRNKDCTAIWEAFKVALDKDPC
SVLPSDYDLFITLSRHSIPRDKSLFWENSHLLVNSFADNTRRFMPLSDVL
YGRVADFLSWCRQKADSGLDYQSCPTSEDCENNPVDSFWKRASIQYSKDS
SGVIHVMLNGSEPTGAYPIKGFFADYEIPNLQKEKITRIEIWVMHEIGGP
NVESCGEGSMKVLEKRLKDMGFQYSCINDYRPVKLLQCVDHSTHPDCALK
Ligand information
Ligand IDENQ
InChIInChI=1S/C17H23N5O14P2/c23-10-7(3-32-37(28,29)36-38(30,31)33-4-8-11(24)13(26)17(27)35-8)34-16(12(10)25)22-6-19-9-14-18-1-2-21(14)5-20-15(9)22/h1-2,5-8,10-13,16-17,23-27H,3-4H2,(H2,28,29,30,31)/p-1/t7-,8-,10-,11-,12-,13-,16-,17-/m1/s1
InChIKeyYOABXPSQFWZTMU-QJWJOKBXSA-M
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.5c1c[n+]2cnc3c(c2[nH]1)ncn3[C@H]4[C@@H]([C@@H]([C@H](O4)COP(=O)([O-])OP(=O)([O-])OC[C@@H]5[C@H]([C@H]([C@@H](O5)O)O)O)O)O
CACTVS 3.385O[C@@H]1O[C@H](CO[P]([O-])(=O)O[P]([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n3cnc4c5[nH]cc[n+]5cnc34)[C@@H](O)[C@H]1O
CACTVS 3.385O[CH]1O[CH](CO[P]([O-])(=O)O[P]([O-])(=O)OC[CH]2O[CH]([CH](O)[CH]2O)n3cnc4c5[nH]cc[n+]5cnc34)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.5c1c[n+]2cnc3c(c2[nH]1)ncn3C4C(C(C(O4)COP(=O)([O-])OP(=O)([O-])OCC5C(C(C(O5)O)O)O)O)O
FormulaC17 H22 N5 O14 P2
Name[[(2R,3S,4R,5R)-3,4-dihydroxy-5-(9H-imidazo[2,1-f]purin-6-ium-3-yl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-3,4-dihydroxy-5-oxidanidyl-oxolan-2-yl]methyl phosphate
ChEMBL
DrugBank
ZINC
PDB chain1isi Chain B Residue 2002 [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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PDB1isi Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		W77 H81 D107 F108 W140 F173
Binding residue
(residue number reindexed from 1)		W76 H80 D106 F107 W139 F172
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) S98 F173 E178
Catalytic site (residue number reindexed from 1) S97 F172 E177
Enzyme Commision number 3.2.2.6: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
Gene Ontology
Molecular Function
GO:0003953 NAD+ nucleosidase activity
GO:0016740 transferase activity
GO:0016787 hydrolase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016849 phosphorus-oxygen lyase activity
GO:0061809 NAD+ nucleotidase, cyclic ADP-ribose generating
Biological Process
GO:0001952 regulation of cell-matrix adhesion
GO:0002691 regulation of cellular extravasation
GO:0006959 humoral immune response
GO:0007165 signal transduction
GO:0008284 positive regulation of cell population proliferation
GO:0030890 positive regulation of B cell proliferation
GO:0032956 regulation of actin cytoskeleton organization
GO:0050727 regulation of inflammatory response
GO:0050730 regulation of peptidyl-tyrosine phosphorylation
GO:0050848 regulation of calcium-mediated signaling
GO:0090022 regulation of neutrophil chemotaxis
GO:0090322 regulation of superoxide metabolic process
GO:2001044 regulation of integrin-mediated signaling pathway
Cellular Component
GO:0001931 uropod
GO:0005576 extracellular region
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0035579 specific granule membrane
GO:0070062 extracellular exosome
GO:0098552 side of membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1isi, PDBe:1isi, PDBj:1isi
PDBsum1isi
PubMed11866528
UniProtQ10588|BST1_HUMAN ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2 (Gene Name=BST1)

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