PDBe 4h1d

X-ray diffraction
2.9Å resolution

Cocrystal structure of GlpG and DFP

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

Assemblies composition:
monomeric (preferred)
homo hexamer
homo trimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhomboid protease GlpG Chain: A
Molecule details ›
Chain: A
Length: 179 amino acids
Theoretical weight: 20.21 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P09391 (Residues: 92-270; Coverage: 65%)
Gene names: JW5687, b3424, glpG
Structure domains: Rhomboid-like domains

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: R32
Unit cell:
a: 110.073Å b: 110.073Å c: 123.995Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.232 0.269
Expression system: Escherichia coli