› 3bii

X-ray diffraction
2.5Å resolution

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:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151796 (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: 8.78 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: 149 amino acids
Theoretical weight: 16.87 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P30749 (Residues: 2-150; Coverage: 99%)
Gene names: JW0768, b0785, chlA5, moaE
Sequence domains: MoaE protein
Structure domains: Molybdopterin biosynthesis MoaE subunit

Ligands and Environments

1 bound ligand:
Ligand CL 4 x CL
1 modified residue:
Ligand GL3 1 x GL3

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: C2
Unit cell:
a: 64.796Å b: 48.735Å c: 74.915Å
α: 90° β: 107.77° γ: 90°
R-values:
R R work R free
0.192 0.189 0.261
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Molybdenum cofactors, enzymes and pathways.
Schwarz et al. (2009)
5 more

20 mentions without citation

A Three-Ring Circus: Metabolism of the Three Proteogenic Aromatic Amino Acids and Their Role in the Health of Plants and Animals.
Parthasarathy et al. (2018)
19 more