X-ray diffraction
2.2Å resolution

Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae


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

Assemblies composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Rhomboid protease GlpG Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 22.14 KDa
Source organism: Haemophilus influenzae 86-028NP
Expression system: Escherichia coli
  • Canonical: P44783 (Residues: 1-192; Coverage: 100%)
Gene names: HI_0618, glpG
Sequence domains: Rhomboid family
Structure domains: Rhomboid-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 121.288Å b: 35.047Å c: 52.931Å
α: 90° β: 104.02° γ: 90°
R R work R free
0.236 0.233 0.295
Expression system: Escherichia coli