› 1di6

X-ray diffraction
1.45Å resolution

1.45 A CRYSTAL STRUCTURE OF THE MOLYBDENUMM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1di6/pdb
PDB entry 1di6 coloured by chain, front view.
PDB entry 1di6 coloured by chain, side view.
PDB entry 1di6 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli.
Liu MT, Wuebbens MM, Rajagopalan KV, Schindelin H
J Biol Chem 275 1814-22 (2000)
PMID: 10636880

Function and Biology Details

Reaction catalysed: 
ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142684 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Molybdopterin adenylyltransferase Chain: A
Molecule details ›
Chain: A
Length: 195 amino acids
Theoretical weight: 21.2 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AF03 (Residues: 1-195; Coverage: 100%)
Gene names: JW0008, b0009, chlG, mog, mogA, yaaG
Sequence domains: Probable molybdopterin binding domain
Structure domains: MoaB/Mog-like domain

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P63
Unit cell:
a: 65.3Å b: 65.3Å c: 65.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.187 0.213
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The mononuclear molybdenum enzymes.
Hille et al. (2014)
4 more

5 mentions without citation

Function of Molybdenum Insertases.
Kruse T. (2022)
4 more