X-ray diffraction
2.1Å resolution

Crystal structure of tm0922, a fusion of a domain of unknown function and ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Thermotoga maritima soaked with NAD and ATP.


Function and Biology Details

Reactions catalysed:
ADP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate + NADH
(6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexadecamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bifunctional NAD(P)H-hydrate repair enzyme Nnr Chain: A
Molecule details ›
Chain: A
Length: 502 amino acids
Theoretical weight: 54.53 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q9X024 (Residues: 1-490; Coverage: 100%)
Gene names: TM_0922, nnr
Sequence domains:
Structure domains:
Unknown peptide, probably from expression host Chain: B
Molecule details ›
Chain: B
Length: 8 amino acids
Theoretical weight: 904 Da
Source organism: Escherichia coli BL21(DE3)

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: I422
Unit cell:
a: 122.399Å b: 122.399Å c: 155.122Å
α: 90° β: 90° γ: 90°
R R work R free
0.171 0.169 0.209
Expression system: Escherichia coli BL21(DE3)