› 5f5g

X-ray diffraction
2.3Å resolution

Structure of E.Coli GlpG Y205F mutant complexed with peptidic inhibitor Ac-RMA-CHO in the DMPC/CHAPSO bicelle

Released:
DOI: 10.2210/pdb5f5g/pdb
Model geometry
Fit model/data
PDB entry 5f5g coloured by chain, front view.
PDB entry 5f5g coloured by chain, side view.
PDB entry 5f5g coloured by chain, top view.
Source organisms:
Primary publication:
Crystal Structures and Inhibition Kinetics Reveal a Two-Stage Catalytic Mechanism with Drug Design Implications for Rhomboid Proteolysis.
Cho S, Dickey SW, Urban S
Mol Cell 61 329-340 (2016)
PMID: 26805573

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:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140632 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Rhomboid protease GlpG Chain: A
Molecule details ›
Chain: A
Length: 211 amino acids
Theoretical weight: 23.8 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P09391 (Residues: 87-276; Coverage: 69%)
Gene names: JW5687, b3424, glpG
Sequence domains: Rhomboid domain
Structure domains: Rhomboid-like
ACE-ARG-MET-ALA-aldehyde Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 388 Da
Source organism: Drosophila melanogaster
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand 5XU 1 x 5XU

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: CHESS BEAMLINE F1
Spacegroup: C2221
Unit cell:
a: 70.83Å b: 97.5Å c: 62.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.255
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

7 review citations

Intramembrane proteases as drug targets.
Verhelst SHL. (2017)
6 more

2 mentions without citation

Crystal Structures and Inhibition Kinetics Reveal a Two-Stage Catalytic Mechanism with Drug Design Implications for Rhomboid Proteolysis.
Cho et al. (2016)
1 more