2ide

X-ray diffraction
1.9Å resolution

Crystal Structure of the molybdenum cofactor biosynthesis protein C (TTHA1789) from Thermus Theromophilus HB8

Released:
Source organism: Thermus thermophilus HB8
Entry authors: Jeyakanthan J, Kanaujia SP, Vasuki Ranjani C, Sekar K, Baba S, Ebihara A, Kuramitsu S, Shinkai A, Shiro Y, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-177865 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclic pyranopterin monophosphate synthase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 157 amino acids
Theoretical weight: 16.95 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SHE1 (Residues: 1-157; Coverage: 100%)
Gene names: TTHA1789, moaC
Sequence domains: MoaC family
Structure domains: Molybdopterin cofactor biosynthesis C (MoaC) domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P21
Unit cell:
a: 64.809Å b: 109.836Å c: 115.192Å
α: 90° β: 104.86° γ: 90°
R-values:
R R work R free
0.195 0.195 0.226
Expression system: Escherichia coli BL21(DE3)