› 1pq8

X-ray diffraction
1Å resolution

Trypsin at pH 4 at atomic resolution

Released:
DOI: 10.2210/pdb1pq8/pdb
PDB entry 1pq8 coloured by chain, front view.
PDB entry 1pq8 coloured by chain, side view.
PDB entry 1pq8 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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152784 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trypsin Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 22.2 KDa
Source organism: Fusarium oxysporum
UniProt:
  • Canonical: P35049 (Residues: 25-248; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
GLY-GLY-ARG PEPTIDE Chain: C
Molecule details ›
Chain: C
Length: 3 amino acids
Theoretical weight: 289 Da
Source organism: Fusarium oxysporum
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand SO4 3 x SO4
Ligand LYS 1 x LYS
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P1
Unit cell:
a: 32.93Å b: 36.887Å c: 39.744Å
α: 102.67° β: 104.66° γ: 102.61°
R-values:
R R work R free
0.128 0.128 not available
Expression system: Not provided

Quick links

Citations

2 review citations

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

2 mentions without citation

Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state.
Blankenship et al. (2014)
1 more