Structure of PDB 1ee1 Chain A

Receptor sequence

>1ee1A (length=271) Species: 1423 (Bacillus subtilis)

SMQEKIMRELHVKPSIDPKQEIEDRVNFLKQYVKKTGAKGFVLGISGGQD
STLAGRLAQLAVESIREEGGDAQFIAVRLPHGTQQDEDDAQLALKFIKPD
KSWKFDIKSTVSAFSDQYQQETGDQLTDFNKGNVKARTRMIAQYAIGGQE
GLLVLGTDHAAEAVTGFFTKYGDGGADLLPLTGLTKRQGRTLLKELGAPE
RLYLKEPTADLLDEKPQQSDETELGISYDEIDDYLEGKEVSAKVSEALEK
RYSMTEHKRQVPASMFDDWWK

3D structure

• PDB: 1ee1 Stabilization of active-site loops in NH3-dependent NAD+ synthetase from Bacillus subtilis.
• Chain: A
• Resolution: 2.06 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	DND	A	F129 N133 F167 F168 T169 K170 D173 A209 L211 E223 H257 K258	F129 N133 F167 F168 T169 K170 D173 A209 L211 E223 H257 K258
BS02	ATP	A	G44 I45 S46 G48 D50 S51 R78 L79 Q84 R139 T157 D173 K186 P207 T208	G44 I45 S46 G48 D50 S51 R78 L79 Q84 R139 T157 D173 K186 P207 T208
BS03	DND	A	Y32 T36 Y144 L153 D177	Y32 T36 Y144 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:1ee1, PDBe:1ee1, PDBj:1ee1
• PDBsum: 1ee1
• PubMed: 11375500
• UniProt: P08164|NADE_BACSU NH(3)-dependent NAD(+) synthetase (Gene Name=nadE)