2x60

X-ray diffraction
2.8Å resolution

Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GTP.

Released:

Function and Biology Details

Reaction catalysed:
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-194691 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleotidyl transferase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 336 amino acids
Theoretical weight: 38.66 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9X0C3 (Residues: 1-336; Coverage: 100%)
Gene name: TM_1033
Sequence domains: Nucleotidyl transferase
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 65.926Å b: 79.567Å c: 70.952Å
α: 90° β: 107.75° γ: 90°
R-values:
R R work R free
0.211 0.207 0.267
Expression system: Escherichia coli BL21