Structure of PDB 2qtr Chain A Binding Site BS01

Receptor Information
>2qtr Chain A (length=189) Species: 1392 (Bacillus anthracis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRKIGIIGGTFDPPHYGHLLIANEVYHALNLEEVWFLPNQIPPHKQGRNI
TSVESRLQMLELATEAEEHFSICLEELSRKGPSYTYDTMLQLTKKYPDVQ
FHFIIGGDMVEYLPKWYNIEALLDLVTFVGVARPGYKLRTPYPITTVEIP
EFAVSSSLLRERYKEKKTCKYLLPEKVQVYIERNGLYES
Ligand information
Ligand IDDND
InChIInChI=1S/C21H26N6O15P2/c22-17-12-18(24-7-23-17)27(8-25-12)20-16(31)14(29)11(41-20)6-39-44(36,37)42-43(34,35)38-5-10-13(28)15(30)19(40-10)26-3-1-2-9(4-26)21(32)33/h1-4,7-8,10-11,13-16,19-20,28-31H,5-6H2,(H4-,22,23,24,32,33,34,35,36,37)/p+1/t10-,11-,13-,14-,15-,16-,19-,20-/m1/s1
InChIKeySENPVEZBRZQVST-HISDBWNOSA-O
SMILES
SoftwareSMILES
CACTVS 3.385Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)OC[C@H]4O[C@H]([C@H](O)[C@@H]4O)[n+]5cccc(c5)C(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.7.6c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O)OP(=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)O
CACTVS 3.385Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH]([CH](O)[CH]4O)[n+]5cccc(c5)C(O)=O)[CH](O)[CH]3O
OpenEye OEToolkits 1.7.6c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)O
FormulaC21 H27 N6 O15 P2
NameNICOTINIC ACID ADENINE DINUCLEOTIDE;
DEAMIDO-NAD+
ChEMBL
DrugBankDB04099
ZINCZINC000008216447
PDB chain2qtr Chain A Residue 191 [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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PDB2qtr Kinetic and X-ray structural evidence for negative cooperativity in substrate binding to nicotinate mononucleotide adenylyltransferase (NMAT) from Bacillus anthracis.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		G8 G9 T10 H18 P43 H44 Y84 T85 G106 D108 M109 W116 R133 F152 V154
Binding residue
(residue number reindexed from 1)		G8 G9 T10 H18 P43 H44 Y84 T85 G106 D108 M109 W116 R133 F152 V154
Annotation score5
Binding affinityMOAD: Kd=3.2uM
Enzymatic activity
Enzyme Commision number 2.7.7.18: nicotinate-nucleotide adenylyltransferase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004515 nicotinate-nucleotide adenylyltransferase activity
GO:0005524 ATP binding
GO:0016779 nucleotidyltransferase activity
GO:0070566 adenylyltransferase activity
Biological Process
GO:0009058 biosynthetic process
GO:0009165 nucleotide biosynthetic process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2qtr, PDBe:2qtr, PDBj:2qtr
PDBsum2qtr
PubMed18977360
UniProtC3L5T6|NADD_BACAC Probable nicotinate-nucleotide adenylyltransferase (Gene Name=nadD)

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