› 1f9z

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF THE NI(II)-BOUND GLYOXALASE I FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1f9z/pdb
PDB entry 1f9z coloured by chain, front view.
PDB entry 1f9z coloured by chain, side view.
PDB entry 1f9z 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 46.047Å b: 56.478Å c: 46.705Å
α: 90° β: 95.44° γ: 90°
R-values:
R R work R free
0.211 0.205 0.272
Expression system: Escherichia coli

Quick links

Citations

14 review citations

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

15 mentions without citation

Nickel-dependent metalloenzymes.
Boer et al. (2014)
14 more