› 1fuo

X-ray diffraction
1.98Å resolution

FUMARASE C WITH BOUND CITRATE

Released:
DOI: 10.2210/pdb1fuo/pdb
PDB entry 1fuo coloured by chain, front view.
PDB entry 1fuo coloured by chain, side view.
PDB entry 1fuo coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli.
Weaver T, Banaszak L
Biochemistry 35 13955-65 (1996)
PMID: 8909293

Function and Biology Details

Reaction catalysed: 
(S)-malate = fumarate + H(2)O
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-138335 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fumarate hydratase class II Chains: A, B
Molecule details ›
Chains: A, B
Length: 467 amino acids
Theoretical weight: 50.55 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P05042 (Residues: 1-467; Coverage: 100%)
Gene names: JW1603, b1611, fumC
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MLT 2 x MLT
Ligand CIT 2 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 104Å b: 219.9Å c: 86.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.165 0.206
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The TCA cycle and tumorigenesis: the examples of fumarate hydratase and succinate dehydrogenase.
Pollard et al. (2003)
3 more

5 mentions without citation

The TB Structural Genomics Consortium: a decade of progress.
Chim et al. (2011)
4 more