Structure of PDB 2qjt Chain B Binding Site BS03

Receptor Information
>2qjt Chain B (length=344) Species: 263 (Francisella tularensis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MYDISVFIGRFQPFHKGHLHNIIIALQNSKKVIINIGSCFNTPNIKNPFS
FEQRKQMIESDLQVAGIDLDTVVIEPLADYFYQEQKWQDELRKNVYKHAK
NNNSIAIVGHIKDSSSYYIRSFPEWDYIGVDNYKNFNATEFRQKFYNGII
SKQYMCSNDPKLGTYNFLTKFMDTQVYQDLVAENNYVIEYKRLWLKAPFK
PNFVTVDALVIVNDHILMVQRKAHPGKDLWALPGGFLECDETIAQAIIRE
LFEETNINLTHEQLAIAKRCEKVFDYPDRSVRGRTISHVGLFVFDQWPSL
PEINAADDAKDVKWISLGSNIKNICDRMLEDHYQIITILLEECG
Ligand information
Ligand IDAMP
InChIInChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyUDMBCSSLTHHNCD-KQYNXXCUSA-N
SMILES
SoftwareSMILES
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N
ACDLabs 12.01O=P(O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)O)O)O)N
FormulaC10 H14 N5 O7 P
NameADENOSINE MONOPHOSPHATE
ChEMBLCHEMBL752
DrugBankDB00131
ZINCZINC000003860156
PDB chain2qjt 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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PDB2qjt Bifunctional NMN Adenylyltransferase/ADP-Ribose Pyrophosphatase: Structure and Function in Bacterial NAD Metabolism.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		Y190 F203 G235 F236 E250 D308
Binding residue
(residue number reindexed from 1)		Y190 F203 G235 F236 E250 D308
Annotation score4
Enzymatic activity
Enzyme Commision number 2.7.7.1: nicotinamide-nucleotide adenylyltransferase.
3.6.1.-
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000309 nicotinamide-nucleotide adenylyltransferase activity
GO:0003824 catalytic activity
GO:0016779 nucleotidyltransferase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2qjt, PDBe:2qjt, PDBj:2qjt
PDBsum2qjt
PubMed18275811
UniProtQ5NHR1

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