› 1fur

X-ray diffraction
1.95Å resolution

FUMARASE MUTANT H188N WITH BOUND SUBSTRATE L-MALATE AT PUTATIVE ACTIVATOR SITE

Released:
DOI: 10.2210/pdb1fur/pdb
PDB entry 1fur coloured by chain, front view.
PDB entry 1fur coloured by chain, side view.
PDB entry 1fur coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site.
Weaver T, Lees M, Banaszak L
Protein Sci 6 834-42 (1997)
PMID: 9098893

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: 50.52 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

1 bound ligand:
Ligand MLT 2 x MLT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2221
Unit cell:
a: 104.03Å b: 219.32Å c: 86.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 0.209
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Intragenic complementation at the argininosuccinate lyase locus: reconstruction of the active site.
Howell et al. (1998)
1 more

4 mentions without citation

Improved amino acid flexibility parameters.
Smith et al. (2003)
3 more