› 3s8k

X-ray diffraction
1.7Å resolution

Crystal structure of a papaya latex serine protease inhibitor (PPI) at 1.7A resolution

Released:
DOI: 10.2210/pdb3s8k/pdb
PDB entry 3s8k coloured by chain, front view.
PDB entry 3s8k coloured by chain, side view.
PDB entry 3s8k coloured by chain, top view.
Source organism: Carica papaya
Primary publication:
The plasticity of the β-trefoil fold constitutes an evolutionary platform for protease inhibition.
Azarkan M, Martinez-Rodriguez S, Buts L, Baeyens-Volant D, Garcia-Pino A
J Biol Chem 286 43726-43734 (2011)
PMID: 22027836

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160445 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Latex serine proteinase inhibitor Chains: A, B
Molecule details ›
Chains: A, B
Length: 184 amino acids
Theoretical weight: 20.68 KDa
Source organism: Carica papaya
UniProt:
  • Canonical: P80691 (Residues: 1-184; Coverage: 100%)
Sequence domains: Trypsin and protease inhibitor
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
4 bound ligands:
Ligand CO 2 x CO
Ligand NH4 3 x NH4
Ligand GOL 4 x GOL
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 44.262Å b: 81.992Å c: 140.891Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.199

Quick links

Citations

2 review citations

Juggling jobs: roles and mechanisms of multifunctional protease inhibitors in plants.
Grosse-Holz et al. (2016)
1 more

1 mention without citation

The plasticity of the β-trefoil fold constitutes an evolutionary platform for protease inhibition.
Azarkan et al. (2011)