Structure of PDB 1m2j Chain A Binding Site BS02

Receptor Information
>1m2j Chain A (length=249) Species: 2234 (Archaeoglobus fulgidus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDEKLLKTIAESKYLVALTGAGVSAESGIPTFRGKDGLWNRYRPEELANP
QAFAKDPEKVWKWYAWRMEKVFNAQPNKANQAFAELERLGVLKCLITQNV
DDLHERAGSRNVIHLHGSLRVVRCTSCNNSFEVESAPKIPPLPKCDKCGS
LLRPGVVWFGEMLPPDVLDRAMREVERADVIIVAGTSAVVQPAASLPLIV
KQRGGAIIEINPDETPLTPIADYSLRGKAGEVMDELVRHVRKALSLKLN
Ligand information
Ligand IDAPR
InChIInChI=1S/C15H23N5O14P2/c16-12-7-13(18-3-17-12)20(4-19-7)14-10(23)8(21)5(32-14)1-30-35(26,27)34-36(28,29)31-2-6-9(22)11(24)15(25)33-6/h3-6,8-11,14-15,21-25H,1-2H2,(H,26,27)(H,28,29)(H2,16,17,18)/t5-,6-,8-,9-,10-,11-,14-,15-/m1/s1
InChIKeySRNWOUGRCWSEMX-KEOHHSTQSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(OCC3OC(n1c2ncnc(N)c2nc1)C(O)C3O)OP(=O)(O)OCC4OC(O)C(O)C4O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)O)O)O)O)O)N
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)O)O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH](O)[CH](O)[CH]4O)[CH](O)[CH]3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P@@](O)(=O)OC[C@H]4O[C@@H](O)[C@H](O)[C@@H]4O)[C@@H](O)[C@H]3O
FormulaC15 H23 N5 O14 P2
NameADENOSINE-5-DIPHOSPHORIBOSE
ChEMBLCHEMBL1231026
DrugBank
ZINCZINC000017654550
PDB chain1m2j Chain A Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1m2j Structural basis for the NAD-dependent deacetylase mechanism of Sir2
Resolution1.7 Å
Binding residue
(original residue number in PDB)		G20 A21 G22 E26 F32 R33 Q98 H116 G185 T186 S187 V190 N211 P212 D213 K228 A229
Binding residue
(residue number reindexed from 1)		G20 A21 G22 E26 F32 R33 Q98 H116 G185 T186 S187 V190 N211 P212 D213 K228 A229
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) P30 T31 F32 R33 N99 D101 H116
Catalytic site (residue number reindexed from 1) P30 T31 F32 R33 N99 D101 H116
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:0036054 protein-malonyllysine demalonylase activity
GO:0036055 protein-succinyllysine desuccinylase activity
GO:0046872 metal ion binding
GO:0070403 NAD+ binding
Biological Process
GO:0006338 chromatin remodeling
GO:0006476 protein deacetylation
GO:0036048 protein desuccinylation
GO:0036049 peptidyl-lysine desuccinylation
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:1m2j, PDBe:1m2j, PDBj:1m2j
PDBsum1m2j
PubMed12091395
UniProtO28597|NPD1_ARCFU NAD-dependent protein deacylase 1 (Gene Name=cobB1)

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