› 1h4d

X-ray diffraction
1.74Å resolution

Biochemical and Structural Analysis of the Molybdenum Cofactor Biosynthesis protein MobA

Released:
DOI: 10.2210/pdb1h4d/pdb
PDB entry 1h4d coloured by chain, front view.
PDB entry 1h4d coloured by chain, side view.
PDB entry 1h4d coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobA.
Guse A, Stevenson CE, Kuper J, Buchanan G, Schwarz G, Giordano G, Magalon A, Mendel RR, Lawson DM, Palmer T
J Biol Chem 278 25302-7 (2003)
PMID: 12719427

Function and Biology Details

Reaction catalysed: 
GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Molybdenum cofactor guanylyltransferase Chain: A
Molecule details ›
Chain: A
Length: 201 amino acids
Theoretical weight: 22.64 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P32173 (Residues: 1-194; Coverage: 100%)
Gene names: JW3829, b3857, chlB, mob, mobA, narB
Sequence domains: MobA-like NTP transferase domain
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

2 bound ligands:
Ligand LI 1 x LI
Ligand CIT 2 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P21212
Unit cell:
a: 76.56Å b: 41.962Å c: 54.319Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 0.219
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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