Structure of PDB 2qjo Chain B Binding Site BS02

Receptor Information
>2qjo Chain B (length=336) Species: 1148 (Synechocystis sp. PCC 6803) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KYQYGIYIGRFQPFHLGHLRTLNLALEKAEQVIIILGSHRVAADTRNPWR
SPERMAMIEACLSPQILKRVHFLTVRDWLYSDNLWLAAVQQQVLKITGGS
NSVVVLGHRKDASSYYLNLFPQWDYLETGHYPDFSSTAIRGAYFEGKEGD
YLDKVPPAIADYLQTFQKSERYIALCDEYQFLQAYKQAWATAPYAPTFIT
TDAVVVQAGHVLMVRRQAKPGLGLIALPGGFIKQNETLVEGMLRELKEET
RLKVPLPVLRGSIVDSHVFDAPGRSLRGRTITHAYFIQLPGGELPAVKGG
DDAQKAWWMSLADLYAQEEQIYEDHFQIIQHFVSKV
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain2qjo Chain B Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)		Y10 I11 G12 R13 H21 G40 S41 D80 W81 D85 W88 H111 K113 Y118 Y119 H133 Y134
Binding residue
(residue number reindexed from 1)		Y7 I8 G9 R10 H18 G37 S38 D77 W78 D82 W85 H108 K110 Y115 Y116 H130 Y131
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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