3rpf

X-ray diffraction
1.9Å resolution

Protein-protein complex of subunit 1 and 2 of Molybdopterin-converting factor from Helicobacter pylori 26695

Released:
Source organism: Helicobacter pylori 26695
Entry authors: Nocek B, Stein A, Marshall N, Jedrzejczak R, Babnigg G, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
Cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + H(2)O = molybdopterin + 2 [molybdopterin-synthase sulfur-carrier protein]
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-127754 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Molybdopterin synthase catalytic subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 148 amino acids
Theoretical weight: 16.99 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli
UniProt:
  • Canonical: P56422 (Residues: 2-145; Coverage: 99%)
Gene names: HP_0800, moaE
Sequence domains: MoaE protein
Structure domains: Molybdopterin biosynthesis MoaE subunit
Molybdopterin converting factor, subunit 1 (MoaD) Chains: C, D
Molecule details ›
Chains: C, D
Length: 74 amino acids
Theoretical weight: 8.38 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli
UniProt:
  • Canonical: O25482 (Residues: 1-74; Coverage: 100%)
Gene name: HP_0801
Sequence domains: ThiS family
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: F222
Unit cell:
a: 88.187Å b: 127.582Å c: 187.945Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.242
Expression system: Escherichia coli