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5b53

X-ray diffraction
2.91Å resolution

Crystal structure of hydrogen sulfide-producing enzyme (Fn1055) from Fusobacterium nucleatum

Released:
Model geometry
Fit model/data
Entry authors: Kezuka Y, Yoshida Y, Nonaka T

Function and Biology Details

Reaction catalysed:
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-185979 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan synthase beta chain-like PALP domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 37.59 KDa
Source organism: Fusobacterium nucleatum subsp. nucleatum ATCC 25586
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8REP3 (Residues: 2-336; Coverage: 100%)
Gene name: FN1055
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P4322
Unit cell:
a: 58.793Å b: 58.793Å c: 205.053Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.171 0.266
Expression system: Escherichia coli BL21(DE3)