› 1trm

X-ray diffraction
2.3Å resolution

THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS

Released:
DOI: 10.2210/pdb1trm/pdb
PDB entry 1trm coloured by chain, front view.
PDB entry 1trm coloured by chain, side view.
PDB entry 1trm coloured by chain, top view.
Source organism: Rattus rattus
Primary publication:
The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis.
Sprang S, Standing T, Fletterick RJ, Stroud RM, Finer-Moore J, Xuong NH, Hamlin R, Rutter WJ, Craik CS
Science 237 905-9 (1987)
PMID: 3112942

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 223 amino acids
Theoretical weight: 23.81 KDa
Source organism: Rattus rattus
Expression system: Not provided
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 CA 2 x CA
Ligand BEN 2 x BEN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 40.4Å b: 92Å c: 127.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 not available not available
Expression system: Not provided

Quick links

Citations

15 review citations

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

5 mentions without citation

Deep Learning in Protein Structural Modeling and Design.
Gao et al. (2020)
4 more