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Receptor Information

>1ifx Chain B (length=245) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

SMQEKIMRELHVKPSIDPKQEIEDRVNFLKQYVKKTGAKGFVLGISGGQD
STLAGRLAQLAVESIREEGGDAQFIAVRLPHGDDAQLALKFIKPDKSWKF
DIKSTVSAFSDQYQQETGDQLTDFNKGNVKARTRMIAQYAIGGQEGLLVL
GTDHAAEAVTGFFTKYGDGGADLLPLTGLTKRQGRTLLKELGAPERLYLI
SYDEIDDYLEGKEVSAKVSEALEKRYSMTEHKRQVPASMFDDWWK

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

1ifx Chain B Residue 7000 [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	1ifx Stabilization of active-site loops in NH3-dependent NAD+ synthetase from Bacillus subtilis.
Resolution	2.25 Å
Binding residue (original residue number in PDB)	F1129 N1133 F1167 F1168 T1169 K1170 D1173 H1257 K1258
Binding residue (residue number reindexed from 1)	F124 N128 F162 F163 T164 K165 D168 H231 K232
Annotation score	5

Catalytic site (original residue number in PDB)	D1050 E1162
Catalytic site (residue number reindexed from 1)	D50 E157
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
GO:0030435	sporulation resulting in formation of a cellular spore

	Cellular Component
GO:0005737	cytoplasm

PDB	RCSB:1ifx, PDBe:1ifx, PDBj:1ifx
PDBsum	1ifx
PubMed	11375500
UniProt	P08164\|NADE_BACSU NH(3)-dependent NAD(+) synthetase (Gene Name=nadE)

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Structure of PDB 1ifx Chain B Binding Site BS02