4u9p

X-ray diffraction
1.7Å resolution

Structure of the methanofuran/methanopterin biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii

Released:

Function and Biology Details

Reaction catalysed:
2 D-glyceraldehyde 3-phosphate = (5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H(2)O
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-176630 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
(5-formylfuran-3-yl)methyl phosphate synthase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 242 amino acids
Theoretical weight: 26.09 KDa
Source organism: Methanocaldococcus jannaschii DSM 2661
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q58499 (Residues: 1-235; Coverage: 100%)
Gene names: MJ1099, mfnB
Sequence domains: 4-HFC-P synthase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2221
Unit cell:
a: 64.76Å b: 152.6Å c: 153.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.202 0.223
Expression system: Escherichia coli BL21(DE3)