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Receptor Information

>1xng Chain B (length=262) Species: 210 (Helicobacter pylori) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

KDYQKLIVYLCDFLEKEVQKRGFKKVVYGLSGGLDSAVVGVLCQKVFKEN
AHALLMPSSVSMPENKTDALNLCEKFSIPYTEYSIAPYDAIFSSHFKDAS
LTRKGNFCARLRMAFLYDYSLKSDSLVIGTSNKSERMLGYGTLFGDLACA
INPIGELFKTEVYELARRLNIPKKILNKPPSADLFVGQSDEKDLGYPYSV
IDPLLKDIEALFQTKPIDTETLAQLGYDEILVKNITSRIQKNAFKLELPA
IAKRFNPELEHH

Ligand ID

DND

InChI

InChI=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

InChIKey

SENPVEZBRZQVST-HISDBWNOSA-O

SMILES

Software	SMILES
CACTVS 3.385	Nc1ncnc2n(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 1.7.6	c1cc(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 3.385	Nc1ncnc2n(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 1.7.6	c1cc(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

Formula

C21 H27 N6 O15 P2

Name

NICOTINIC ACID ADENINE DINUCLEOTIDE;
DEAMIDO-NAD+

PDB chain

1xng Chain B Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1xng Crystal structure of NH3-dependent NAD+ synthetase from Helicobacter pylori
Resolution	1.7 Å
Binding residue (original residue number in PDB)	N108 Y142 G143 T144 D148 A184 F246 K247
Binding residue (residue number reindexed from 1)	N106 Y140 G141 T142 D146 A182 F244 K245
Annotation score	5

Catalytic site (original residue number in PDB)	D37 E137
Catalytic site (residue number reindexed from 1)	D35 E135
Enzyme Commision number	6.3.1.5: NAD(+) synthase.

	Molecular Function
GO:0003952	NAD+ synthase (glutamine-hydrolyzing) activity
GO:0004359	glutaminase activity
GO:0005524	ATP binding
GO:0008795	NAD+ synthase activity
GO:0016874	ligase activity
GO:0046872	metal ion binding

	Biological Process
GO:0009435	NAD biosynthetic process

	Cellular Component
GO:0005737	cytoplasm

PDB	RCSB:1xng, PDBe:1xng, PDBj:1xng
PDBsum	1xng
PubMed	15645437
UniProt	O25096\|NADE_HELPY NH(3)-dependent NAD(+) synthetase (Gene Name=nadE)

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Structure of PDB 1xng Chain B Binding Site BS02