› 1di7

X-ray diffraction
1.6Å resolution

1.60 ANGSTROM CRYSTAL STRUCTURE OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1di7/pdb
PDB entry 1di7 coloured by chain, front view.
PDB entry 1di7 coloured by chain, side view.
PDB entry 1di7 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: 65.5Å b: 65.5Å c: 64.347Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.205 0.226
Expression system: Escherichia coli

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Citations

6 review citations

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