› 1fmg

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.04% POLYDOCANOL

Released:
DOI: 10.2210/pdb1fmg/pdb
PDB entry 1fmg coloured by chain, front view.
PDB entry 1fmg coloured by chain, side view.
PDB entry 1fmg coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Structures of porcine beta-trypsin-detergent complexes: the stabilization of proteins through hydrophilic binding of polydocanol.
Deepthi S, Johnson A, Pattabhi V
Acta Crystallogr D Biol Crystallogr 57 1506-12 (2001)
PMID: 11679713

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypsin Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.49 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P00761 (Residues: 9-231; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

3 bound ligands:
Ligand CA 1 x CA
Ligand SO4 1 x SO4
Ligand EDO 5 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P212121
Unit cell:
a: 77.947Å b: 54.155Å c: 47.274Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.158 0.234

Quick links

Citations

3 citation in other articles

Effect of sorbitol and glycerol on the stability of trypsin and difference between their stabilization effects in the various solvents.
Pazhang et al. (2016)
2 more

2 mentions without citation

PaFlexPepDock: parallel ab-initio docking of peptides onto their receptors with full flexibility based on Rosetta.
Li et al. (2014)
1 more