› 2tga

X-ray diffraction
1.8Å resolution

ON THE DISORDERED ACTIVATION DOMAIN IN TRYPSINOGEN. CHEMICAL LABELLING AND LOW-TEMPERATURE CRYSTALLOGRAPHY

Released:
DOI: 10.2210/pdb2tga/pdb
PDB entry 2tga coloured by chain, front view.
PDB entry 2tga coloured by chain, side view.
PDB entry 2tga coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
On the Disordered Activation Domain in Trypsinogen. Chemical Labelling and Low-Temperature Crystallography
Walter J, Steigemann W, Singh TP, Bartunik H, Bode W, Huber R
Acta Crystallogr., B 38 1462-1472 (1982)

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-133319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease 1 Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 24.01 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00760 (Residues: 18-246; Coverage: 100%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 55.11Å b: 55.11Å c: 109.38Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 not available
Expression system: Not provided

Quick links

Citations

4 mentions without citation

Ligand-binding site prediction of proteins based on known fragment-fragment interactions.
Kasahara et al. (2010)
3 more