PDBe 5kha

X-ray diffraction
2.1Å resolution

Structure of glutamine-dependent NAD+ synthetase from Acinetobacter baumannii in complex with adenosine diphosphate (ADP)

Source organism: Acinetobacter baumannii
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reactions catalysed:
ATP + deamido-NAD(+) + L-glutamine + H(2)O = AMP + diphosphate + NAD(+) + L-glutamate
ATP + deamido-NAD(+) + NH(3) = AMP + diphosphate + NAD(+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Glutamine-dependent NAD(+) synthetase Chains: A, B
Molecule details ›
Chains: A, B
Length: 549 amino acids
Theoretical weight: 61.5 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21(DE3)
  • Canonical: V5VHL3 (Residues: 1-541; Coverage: 100%)
Gene names: A7M79_02695, A7M90_13995, A7N09_01215, ABUW_3069, B9X91_21395, B9X95_06120, BGC29_09355, BWP00_11980, C2U32_18565, C3415_14480, C7G90_15660, CBE85_08710, CBI29_00879, CEJ63_16210, CHQ89_11240, CPI82_11215, DCD76_07200, IX87_01870, NCTC13421_03009, nadE
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 71.88Å b: 123.75Å c: 73.65Å
α: 90° β: 110.93° γ: 90°
R R work R free
0.166 0.165 0.21
Expression system: Escherichia coli BL21(DE3)