› 1o8o

X-ray diffraction
2.7Å resolution

The active site of the molybdenum cofactor biosynthetic protein domain Cnx1G

Released:
DOI: 10.2210/pdb1o8o/pdb
PDB entry 1o8o coloured by chain, front view.
PDB entry 1o8o coloured by chain, side view.
PDB entry 1o8o coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
The active site of the molybdenum cofactor biosynthetic protein domain Cnx1G.
Kuper J, Winking J, Hecht HJ, Mendel RR, Schwarz G
Arch Biochem Biophys 411 36-46 (2003)
PMID: 12590921

Function and Biology Details

Reactions catalysed: 
Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP
ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174429 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Molybdopterin biosynthesis protein CNX1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 167 amino acids
Theoretical weight: 17.73 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q39054 (Residues: 462-628; Coverage: 25%)
Gene names: At5g20990, CNX1, F22D1.6, T10F18.20
Sequence domains: Probable molybdopterin binding domain
Structure domains: MoaB/Mog-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I4122
Unit cell:
a: 122.263Å b: 122.263Å c: 174.623Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.243
Expression system: Escherichia coli

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Citations

4 review citations

Molybdenum cofactor biosynthesis and molybdenum enzymes.
Schwarz et al. (2006)
3 more