X-ray diffraction
2.1Å resolution

Crystal structure of GlpG

Source organism: Escherichia coli
Primary publication:
Crystal structure of a rhomboid family intramembrane protease.
Nature 444 179-80 (2006)
PMID: 17051161

Function and Biology Details

Reaction catalysed:
Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Rhomboid protease GlpG Chain: A
Molecule details ›
Chain: A
Length: 182 amino acids
Theoretical weight: 20.53 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P09391 (Residues: 91-272; Coverage: 66%)
Gene names: JW5687, b3424, glpG
Structure domains: Rhomboid-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: R32
Unit cell:
a: 110.822Å b: 110.822Å c: 127.611Å
α: 90° β: 90° γ: 120°
R R work R free
0.236 0.236 0.252
Expression system: Escherichia coli BL21(DE3)