1fma

X-ray diffraction
1.58Å resolution

MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)

Released:

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 dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-151795 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Molybdopterin synthase sulfur carrier subunit Chain: D
Molecule details ›
Chain: D
Length: 81 amino acids
Theoretical weight: 8.76 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P30748 (Residues: 1-81; Coverage: 100%)
Gene names: JW0767, b0784, chlA4, chlM, moaD
Sequence domains: ThiS family
Structure domains: Ubiquitin-like (UB roll)
Molybdopterin synthase catalytic subunit Chain: E
Molecule details ›
Chain: E
Length: 150 amino acids
Theoretical weight: 17 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P30749 (Residues: 1-150; Coverage: 100%)
Gene names: JW0768, b0785, chlA5, moaE
Sequence domains: MoaE protein
Structure domains: Molybdopterin biosynthesis MoaE subunit

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: C2
Unit cell:
a: 64.15Å b: 47.959Å c: 74.146Å
α: 90° β: 107.35° γ: 90°
R-values:
R R work R free
0.173 0.172 0.218
Expression system: Escherichia coli