Structure of PDB 1kqp Chain B

Receptor sequence

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

SMQEKIMRELHVKPSIDPKQEIEDRVNFLKQYVKKTGAKGFVLGISGGQD
STLAGRLAQLAVESIREEGGDAQFIAVRLPHGTQQDEDDAQLALKFIKPD
KSWKFDIKSTVSAFSDQYQQETGDQLTDFNKGNVKARTRMIAQYAIGGQE
GLLVLGTDHAAEAVTGFFTKYGDGGADLLPLTGLTKRQGRTLLKELGAPE
RLYLKEPTADLLDEKPQQSDETELGISYDEIDDYLEGKEVSAKVSEALEK
RYSMTEHKRQVPASMFDDWWK

3D structure

• PDB: 1kqp NH3-dependent NAD+ synthetase from Bacillus subtilis at 1 A resolution.
• Chain: B
• Resolution: 1.03 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	ADJ	B	Y32 T36 Y144 D177	Y32 T36 Y144 D177
BS02	MG	B	D50 E162	D50 E162
BS03	ADJ	B	G44 I45 S46 S51 L79 Q84 N133 R139 T157 E162 F167 F168 T169 K170 D173 T208 A209 L211 E223 H257 K258	G44 I45 S46 S51 L79 Q84 N133 R139 T157 E162 F167 F168 T169 K170 D173 T208 A209 L211 E223 H257 K258
BS04	POP	B	S46 G48 D50 S51 K186 P207 T208	S46 G48 D50 S51 K186 P207 T208

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:1kqp, PDBe:1kqp, PDBj:1kqp
• PDBsum: 1kqp
• PubMed: 12077433
• UniProt: P08164|NADE_BACSU NH(3)-dependent NAD(+) synthetase (Gene Name=nadE)