› 1and

X-ray diffraction
2.3Å resolution

ANIONIC TRYPSIN MUTANT WITH ARG 96 REPLACED BY HIS

Released:
DOI: 10.2210/pdb1and/pdb
PDB entry 1and coloured by chain, front view.
PDB entry 1and coloured by chain, side view.
PDB entry 1and coloured by chain, top view.
Source organism: Rattus rattus
Primary publication:
Structure of an engineered, metal-actuated switch in trypsin.
McGrath ME, Haymore BL, Summers NL, Craik CS, Fletterick RJ
Biochemistry 32 1914-9 (1993)
PMID: 8448149

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133401 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Anionic trypsin-2 Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.8 KDa
Source organism: Rattus rattus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00763 (Residues: 24-246; Coverage: 97%)
Gene names: Prss2, Try2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand CU 1 x CU
Ligand BEN 1 x BEN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: I23
Unit cell:
a: 124.38Å b: 124.38Å c: 124.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.161 not available
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Structural basis of substrate specificity in the serine proteases.
Perona et al. (1995)
8 more

159 mentions without citation

Peptide signaling in the staphylococci.
Thoendel et al. (2011)
158 more