› 1ezw

X-ray diffraction
1.65Å resolution

STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOPYRUS KANDLERI

Released:
DOI: 10.2210/pdb1ezw/pdb
PDB entry 1ezw coloured by chain, front view.
PDB entry 1ezw coloured by chain, side view.
PDB entry 1ezw coloured by chain, top view.
Source organism: Methanopyrus kandleri
Primary publication:
Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea.
Shima S, Warkentin E, Grabarse W, Sordel M, Wicke M, Thauer RK, Ermler U
J Mol Biol 300 935-50 (2000)
PMID: 10891279

Function and Biology Details

Reaction catalysed: 
5-methyltetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186312 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5,10-methylenetetrahydromethanopterin reductase Chain: A
Molecule details ›
Chain: A
Length: 349 amino acids
Theoretical weight: 37.55 KDa
Source organism: Methanopyrus kandleri
UniProt:
  • Canonical: Q8TXY4 (Residues: 1-349; Coverage: 100%)
Gene names: MK0524, mer
Sequence domains: Luciferase-like monooxygenase
Structure domains: Luciferase-like domain

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: F222
Unit cell:
a: 90.2Å b: 144.1Å c: 152.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.212

Quick links

Citations

4 review citations

Deflavination and reconstitution of flavoproteins.
Hefti et al. (2003)
3 more

9 mentions without citation

Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs.
Tabita et al. (2007)
8 more