› 1qd1

X-ray diffraction
1.7Å resolution

THE CRYSTAL STRUCTURE OF THE FORMIMINOTRANSFERASE DOMAIN OF FORMIMINOTRANSFERASE-CYCLODEAMINASE.

Released:
DOI: 10.2210/pdb1qd1/pdb
PDB entry 1qd1 coloured by chain, front view.
PDB entry 1qd1 coloured by chain, side view.
PDB entry 1qd1 coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme.
Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A
Structure 8 35-46 (2000)
PMID: 10673422

Function and Biology Details

Reactions catalysed: 
5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH(3)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156818 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formimidoyltransferase-cyclodeaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 325 amino acids
Theoretical weight: 35.88 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P53603 (Residues: 2-326; Coverage: 60%)
Gene name: FTCD
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FON 2 x FON
1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200, NSLS BEAMLINE X8C
Spacegroup: P212121
Unit cell:
a: 64.31Å b: 103.84Å c: 122.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.213
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Channeling of substrates and intermediates in enzyme-catalyzed reactions.
Huang et al. (2001)
2 more

1 mention without citation

Channelling and formation of 'active' formaldehyde in dimethylglycine oxidase.
Leys et al. (2003)