1qlm

X-ray diffraction
2Å resolution

The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri

Released:

Function and Biology Details

Reaction catalysed:
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H(2)O = 5-formyl-5,6,7,8-tetrahydromethanopterin
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-161138 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methenyltetrahydromethanopterin cyclohydrolase Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 34.09 KDa
Source organism: Methanopyrus kandleri
Expression system: Escherichia coli
UniProt:
  • Canonical: P94954 (Residues: 1-316; Coverage: 100%)
Gene names: MK0625, mch
Sequence domains: Cyclohydrolase (MCH)
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P6322
Unit cell:
a: 125.9Å b: 125.9Å c: 172.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.198 0.219
Expression system: Escherichia coli