2nrf

X-ray diffraction
2.6Å resolution

Crystal Structure of GlpG, a Rhomboid family intramembrane protease

Released:

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140641 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhomboid protease GlpG Chains: A, B
Molecule details ›
Chains: A, B
Length: 182 amino acids
Theoretical weight: 20.53 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P09391 (Residues: 91-272; Coverage: 66%)
Gene names: JW5687, b3424, glpG
Sequence domains: Rhomboid family
Structure domains: Rhomboid-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P31
Unit cell:
a: 59.458Å b: 59.458Å c: 118.048Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.285 0.262 0.295
Expression system: Escherichia coli