› 4gi3

X-ray diffraction
1.75Å resolution

Crystal structure of Greglin in complex with subtilisin

Released:
DOI: 10.2210/pdb4gi3/pdb
PDB entry 4gi3 coloured by chain, front view.
PDB entry 4gi3 coloured by chain, side view.
PDB entry 4gi3 coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of greglin, a novel non-classical Kazal inhibitor, in complex with subtilisin.
Derache C, Epinette C, Roussel A, Gabant G, Cadene M, Korkmaz B, Gauthier F, Kellenberger C
FEBS J 279 4466-78 (2012)
PMID: 23075397

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160933 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase S8/S53 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 27.44 KDa
Source organism: Bacillus licheniformis
UniProt:
  • Canonical: Q9FDF2 (Residues: 37-310; Coverage: 88%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Greglin Chain: C
Molecule details ›
Chain: C
Length: 83 amino acids
Theoretical weight: 9.2 KDa
Source organism: Schistocerca gregaria
UniProt:
  • Canonical: P85064 (Residues: 1-83; Coverage: 100%)
Structure domains: Wheat Germ Agglutinin (Isolectin 2); domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: C2
Unit cell:
a: 131.07Å b: 39.708Å c: 59.75Å
α: 90° β: 98.05° γ: 90°
R-values:
R R work R free
0.168 0.166 0.201

Quick links

Citations

6 citation in other articles

New selective peptidyl di(chlorophenyl) phosphonate esters for visualizing and blocking neutrophil proteinase 3 in human diseases.
Guarino et al. (2014)
5 more

6 mentions without citation

The discovery of novel heat-stable keratinases from Meiothermus taiwanensis WR-220 and other extremophiles.
Wu et al. (2017)
5 more