Structure of PDB 1nsy Chain A

Receptor sequence

>1nsyA (length=271) Species: 1423 (Bacillus subtilis)

SMQEKIMRELHVKPSIDPKQEIEDRVNFLKQYVKKTGAKGFVLGISGGQD
STLAGRLAQLAVESIREEGGDAQFIAVRLPHGTQQDEDDAQLALKFIKPD
KSWKFDIKSTVSAFSDQYQQETGDQLTDFNKGNVKARTRMIAQYAIGGQE
GLLVLGTDHAAEAVTGFFTKYGDGGADLLPLTGLTKRQGRTLLKELGAPE
RLYLKEPTADLLDEKPQQSDETELGISYDEIDDYLEGKEVSAKVSEALEK
RYSMTEHKRQVPASMFDDWWK

3D structure

• PDB: 1nsy Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D50 E162
• Catalytic site (residue number reindexed from 1): D50 E162
• Enzyme Commision number: 6.3.1.5: NAD(+) synthase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	MG	A	D50 E162	D50 E162
BS02	ATP	A	F129 N133 T169 K170 H257 K258	F129 N133 T169 K170 H257 K258
BS03	AMP	A	G44 I45 S46 L79 Q84 R139 T157 T208 A209	G44 I45 S46 L79 Q84 R139 T157 T208 A209
BS04	POP	A	S46 G48 D50 S51 K186 P207 T208	S46 G48 D50 S51 K186 P207 T208
BS05	ATP	A	Y32 L153 D177	Y32 L153 D177

Gene Ontology

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

External links

• PDB: RCSB:1nsy, PDBe:1nsy, PDBj:1nsy
• PDBsum: 1nsy
• PubMed: 8895556
• UniProt: P08164|NADE_BACSU NH(3)-dependent NAD(+) synthetase (Gene Name=nadE)