PDBe 2irv

X-ray diffraction
2.3Å resolution

Crystal structure of GlpG, a rhomboid intramembrane serine protease

Source organism: Escherichia coli K-12
Primary publication:
Structural basis for intramembrane proteolysis by rhomboid serine proteases.
Proc. Natl. Acad. Sci. U.S.A. 104 462-6 (2007)
PMID: 17190827

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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Rhomboid protease GlpG Chains: A, B
Molecule details ›
Chains: A, B
Length: 182 amino acids
Theoretical weight: 20.56 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
  • Canonical: P09391 (Residues: 92-273; Coverage: 66%)
Gene names: JW5687, b3424, glpG
Sequence domains: Rhomboid family
Structure domains: Rhomboid-like

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 49.82Å b: 69.35Å c: 67.58Å
α: 90° β: 101.03° γ: 90°
R R work R free
0.22 0.22 0.263
Expression system: Escherichia coli