› 1pqa

X-ray diffraction
1.23Å resolution

Trypsin with PMSF at atomic resolution

Released:
DOI: 10.2210/pdb1pqa/pdb
PDB entry 1pqa coloured by chain, front view.
PDB entry 1pqa coloured by chain, side view.
PDB entry 1pqa coloured by chain, top view.
Source organism: Fusarium oxysporum
Primary publication:
Trypsin revisited: crystallography AT (SUB) atomic resolution and quantum chemistry revealing details of catalysis.
Schmidt A, Jelsch C, Ostergaard P, Rypniewski W, Lamzin VS
J Biol Chem 278 43357-62 (2003)
PMID: 12937176

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-152777 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypsin Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 22.35 KDa
Source organism: Fusarium oxysporum
UniProt:
  • Canonical: P35049 (Residues: 25-248; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
1 modified residue:
Ligand SEB 1 x SEB

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 33.066Å b: 66.763Å c: 39.274Å
α: 90° β: 108.02° γ: 90°
R-values:
R R work R free
0.141 0.141 not available

Quick links

Citations

2 review citations

Neutron Laue macromolecular crystallography.
Meilleur et al. (2006)
1 more

5 mentions without citation

Analysis of substructural variation in families of enzymatic proteins with applications to protein function prediction.
Bryant et al. (2010)
4 more