› 1fa8

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF THE APO FORM GLYOXALASE I OF ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1fa8/pdb
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PDB entry 1fa8 coloured by chain, front view.
PDB entry 1fa8 coloured by chain, side view.
PDB entry 1fa8 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation.
He MM, Clugston SL, Honek JF, Matthews BW
Biochemistry 39 8719-27 (2000)
PMID: 10913283

Function and Biology Details

Reaction catalysed: 
(R)-S-lactoylglutathione = glutathione + methylglyoxal
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142248 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lactoylglutathione lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 135 amino acids
Theoretical weight: 14.94 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AC81 (Residues: 1-135; Coverage: 100%)
Gene names: JW1643, b1651, gloA
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 46.275Å b: 57.197Å c: 46.99Å
α: 90° β: 95.24° γ: 90°
R-values:
R R work R free
0.19 0.188 0.255
Expression system: Escherichia coli

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Citations

16 review citations

3D domain swapping: as domains continue to swap.
Liu et al. (2002)
15 more

4 mentions without citation

Nonredox nickel enzymes.
Maroney et al. (2014)
3 more

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