Structure of PDB 2qjo Chain A Binding Site BS01

Receptor Information
>2qjo Chain A (length=332) Species: 1148 (Synechocystis sp. PCC 6803) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DPMQTKYQYGIYIGRFQPFHLGHLRTLNLALEKAEQVIIILGSHRVAADT
RNPWRSPERMAMIEACLSPQILKRVHFLTVRDWLYSDNLWLAAVQQQVLK
ITGGSNSVVVLGHRKDASSYYLNLFPQWDYLETGHYPDFSSTAIRGAYFE
GKEGDYLDKVPPAIADYLQTFQKSERYIALCDEYQFLQAYKQAWATAPYA
PTFITTDAVVVQAGHVLMVRRQAKPGLGLIALPGGFIKQNETLVEGMLRE
LKEETRLKVPLPVLRGSIVDSHVFDAPGRSLRGRTITHAYFIQLPGGELP
AVKKAWWMSLADLYAQEEQIYEDHFQIIQHFV
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 chain2qjo Chain A Residue 501 [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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PDB2qjo Bifunctional NMN Adenylyltransferase/ADP-Ribose Pyrophosphatase: Structure and Function in Bacterial NAD Metabolism.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		Y188 F201 D205 R219 G232 G233 F234 E248 R277 R280 E326 H328
Binding residue
(residue number reindexed from 1)		Y190 F203 D207 R221 G234 G235 F236 E250 R279 R282 E322 H324
Annotation score4
Enzymatic activity
Enzyme Commision number 2.7.7.1: nicotinamide-nucleotide adenylyltransferase.
3.6.1.-
Gene Ontology
Molecular Function
GO:0000309 nicotinamide-nucleotide adenylyltransferase activity
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016779 nucleotidyltransferase activity
GO:0016787 hydrolase activity
GO:0042802 identical protein binding
Biological Process
GO:0009058 biosynthetic process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process
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:2qjo, PDBe:2qjo, PDBj:2qjo
PDBsum2qjo
PubMed18275811
UniProtQ55928|NADM_SYNY3 Bifunctional NMN adenylyltransferase/Nudix hydrolase (Gene Name=slr0787)

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