PDBe 3zmi

X-ray diffraction
2.2Å resolution

Structure of E.coli rhomboid protease GlpG in complex with monobactam L29

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:
monomeric (preferred)
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
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09391 (Residues: 92-270; Coverage: 65%)
Gene names: JW5687, b3424, glpG
Structure domains: Rhomboid-like domains

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: R32
Unit cell:
a: 110.58Å b: 110.58Å c: 128.53Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.216 0.261
Expression system: Escherichia coli BL21(DE3)