Structure of PDB 4bv2 Chain A Binding Site BS05

Receptor Information
>4bv2 Chain A (length=235) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KMKEFLDLLNESRLTVTLTGAGISTPSGIPDFYSQNVFDIDFFYSHPEEF
YRFAKEGIFPMLQAKPNLAHVLLAKLEEKGLIEAVITQNIDRLHQRAGSK
KVIELHGNVEEYYCVRCEKKYTVEDVIKKLESSDVPLCDDCNSLIRPNIV
FFGENLPQDALREAIGLSSRASLMIVLGSSLVVYPAAELPLITVRSGGKL
VIVNLGETPFDDIATLKYNMDVVEFARRVMEEGGI
Ligand information
Ligand IDOAD
InChIInChI=1S/C17H25N5O15P2/c1-6(23)34-13-11(25)8(36-17(13)27)3-33-39(30,31)37-38(28,29)32-2-7-10(24)12(26)16(35-7)22-5-21-9-14(18)19-4-20-15(9)22/h4-5,7-8,10-13,16-17,24-27H,2-3H2,1H3,(H,28,29)(H,30,31)(H2,18,19,20)/t7-,8-,10-,11-,12-,13-,16-,17+/m1/s1
InChIKeyBFNOPXRXIQJDHO-DLFWLGJNSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.5CC(=O)OC1C(C(OC1O)COP(=O)(O)OP(=O)(O)OCC2C(C(C(O2)n3cnc4c3ncnc4N)O)O)O
CACTVS 3.385CC(=O)O[CH]1[CH](O)O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)n3cnc4c(N)ncnc34)[CH]1O
ACDLabs 10.04O=C(OC1C(O)C(OC1O)COP(=O)(O)OP(=O)(O)OCC4OC(n2c3ncnc(N)c3nc2)C(O)C4O)C
OpenEye OEToolkits 1.7.5CC(=O)O[C@@H]1[C@@H]([C@H](O[C@@H]1O)CO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]2[C@H]([C@H]([C@@H](O2)n3cnc4c3ncnc4N)O)O)O
CACTVS 3.385CC(=O)O[C@H]1[C@@H](O)O[C@H](CO[P](O)(=O)O[P](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n3cnc4c(N)ncnc34)[C@H]1O
FormulaC17 H25 N5 O15 P2
Name2'-O-ACETYL ADENOSINE-5-DIPHOSPHORIBOSE
ChEMBL
DrugBankDB03478
ZINCZINC000058638658
PDB chain4bv2 Chain A Residue 1248 [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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PDB4bv2 Ex-527 Inhibits Sirtuins by Exploiting Their Unique Nad+-Dependent Deacetylation Mechanism
Resolution3.3 Å
Binding residue
(original residue number in PDB)		G21 A22 G23 T26 P27 F33 Q98 H116 F162 S189 S190 N214 L215 M230 D231 V232
Binding residue
(residue number reindexed from 1)		G20 A21 G22 T25 P26 F32 Q88 H106 F152 S179 S180 N204 L205 M220 D221 V222
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) P31 D32 F33 N99 D101 H116
Catalytic site (residue number reindexed from 1) P30 D31 F32 N89 D91 H106
Enzyme Commision number 2.3.1.286: protein acetyllysine N-acetyltransferase.
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016740 transferase activity
GO:0017136 NAD-dependent histone deacetylase activity
GO:0034979 NAD-dependent protein lysine deacetylase activity
GO:0046872 metal ion binding
GO:0051287 NAD binding
GO:0070403 NAD+ binding
Biological Process
GO:0006338 chromatin remodeling
GO:0006476 protein deacetylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4bv2, PDBe:4bv2, PDBj:4bv2
PDBsum4bv2
PubMed23840057
UniProtQ9WYW0|NPD_THEMA NAD-dependent protein deacetylase (Gene Name=cobB)

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