› 2fhk

X-ray diffraction
2Å resolution

Crystal structure of formylmethanofuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes

Released:
DOI: 10.2210/pdb2fhk/pdb
PDB 2fhk coloured by chain and viewed from the front.
PDB 2fhk coloured by chain and viewed from the side.
PDB 2fhk coloured by chain and viewed from the top.
Source organism: Methanopyrus kandleri
Primary publication:
The structure of formylmethanofuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes.
Acharya P, Warkentin E, Ermler U, Thauer RK, Shima S
J. Mol. Biol. 357 870-9 (2006)
PMID: 16466742

Function and Biology Details

Reaction catalysed: 
Formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formylmethanofuran--tetrahydromethanopterin formyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 296 amino acids
Theoretical weight: 31.69 KDa
Source organism: Methanopyrus kandleri
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q49610 (Residues: 1-296; Coverage: 100%)
Gene names: MK0116, ftr
Sequence domains:
Structure domains: Alpha-Beta Plaits

Ligands and Environments

2 bound ligands:
Ligand K 18 x K
Ligand MFN 3 x MFN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 86Å b: 74.2Å c: 103.6Å
α: 90° β: 113.6° γ: 90°
R-values:
R R work R free
0.219 0.218 0.245
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Coenzymes and Their Role in the Evolution of Life.
Kirschning A. (2021)
2 more