› 1amh

X-ray diffraction
2.5Å resolution

UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)

Released:
DOI: 10.2210/pdb1amh/pdb
PDB entry 1amh coloured by chain, front view.
PDB entry 1amh coloured by chain, side view.
PDB entry 1amh coloured by chain, top view.
Source organism: Rattus rattus
Primary publication:
The three-dimensional structure of Asp189Ser trypsin provides evidence for an inherent structural plasticity of the protease.
Szabó E, Böcskei Z, Náray-Szabó G, Gráf L
Eur J Biochem 263 20-6 (1999)
PMID: 10429182

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: 23.79 KDa
Source organism: Rattus rattus
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00763 (Residues: 24-246; Coverage: 97%)
Gene names: Prss2, Try2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 45.92Å b: 49.79Å c: 89.88Å
α: 90° β: 97.34° γ: 90°
R-values:
R R work R free
0.182 0.182 0.242
Expression system: Saccharomyces cerevisiae

Quick links

Citations

1 review citation

Minor structural changes, major functional impacts: posttranslational modifications and drug targets.
Kim HJ. (2022)
16 other articles

1 mention without citation

Mechanisms and specificity of factor XIa and trypsin inhibition by protease nexin 2 and basic pancreatic trypsin inhibitor.
Navaneetham et al. (2010)