2ax3

X-ray diffraction
2.27Å resolution

CRYSTAL STRUCTURE OF A PUTATIVE CARBOHYDRATE KINASE (TM0922) FROM THERMOTOGA MARITIMA MSB8 AT 2.25 A RESOLUTION

Released:
Source organism: Thermotoga maritima MSB8
Entry author: Joint Center for Structural Genomics (JCSG)

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

Assemblies composition:
hetero hexadecamer
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-162632 (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: 54.9 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X024 (Residues: 1-490; Coverage: 100%)
Gene names: TM_0922, nnr
Sequence domains:
Structure domains:
unknown peptide Chain: B
Molecule details ›
Chain: B
Length: 8 amino acids
Theoretical weight: 915 Da
Source organism: Thermotoga maritima MSB8
Expression system: Not provided

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: I422
Unit cell:
a: 121.264Å b: 121.264Å c: 153.873Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.159 0.218
Expression systems:
  • Escherichia coli
  • Not provided