PDBe 3zot

X-ray diffraction
2.4Å resolution

Structure of E.coli rhomboid protease GlpG in complex with monobactam L29 (data set 2)


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 Chain: A
Molecule details ›
Chain: A
Length: 180 amino acids
Theoretical weight: 20.33 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P09391 (Residues: 92-271; Coverage: 65%)
Gene names: JW5687, b3424, glpG
Structure domains: Rhomboid-like

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: R32
Unit cell:
a: 110.2Å b: 110.2Å c: 128.9Å
α: 90° β: 90° γ: 120°
R R work R free
0.201 0.198 0.252
Expression system: Escherichia coli BL21(DE3)