3txt

X-ray diffraction
2.3Å resolution

Crystal structure of GlpG in complex with inhibitor DFP

Released:
Source organism: Escherichia coli K-12
Entry authors: Xue Y, Ha Y

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 trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140642 (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 K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P09391 (Residues: 92-270; Coverage: 65%)
Gene names: JW5687, b3424, glpG
Sequence domains: Rhomboid family
Structure domains: Rhomboid-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: R32
Unit cell:
a: 109.667Å b: 109.667Å c: 125.097Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.219 0.238
Expression system: Escherichia coli