1vp2

X-ray diffraction
1.78Å resolution

CRYSTAL STRUCTURE OF A PUTATIVE XANTHOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN HOMOLOG (TM0159) FROM THERMOTOGA MARITIMA AT 1.78 A RESOLUTION

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

Function and Biology Details

Reaction catalysed:
ITP + H(2)O = IMP + diphosphate

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dITP/XTP pyrophosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 23.83 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WY06 (Residues: 1-196; Coverage: 100%)
Gene name: TM_0159
Sequence domains: Ham1 family
Structure domains: Maf protein

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P41212
Unit cell:
a: 142.851Å b: 142.851Å c: 45.082Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.205
Expression system: Escherichia coli