› 1y3x

X-ray diffraction
1.7Å resolution

TRYPSIN INHIBITOR COMPLEX

Released:
DOI: 10.2210/pdb1y3x/pdb
PDB entry 1y3x coloured by chain, front view.
PDB entry 1y3x coloured by chain, side view.
PDB entry 1y3x coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
A simple protocol to estimate differences in protein binding affinity for enantiomers without prior resolution of racemates.
Fokkens J, Klebe G
Angew Chem Int Ed Engl 45 985-9 (2006)
PMID: 16374786

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: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand UIB 1 x UIB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 63.25Å b: 69.3Å c: 63.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.152 0.204

Quick links

Citations

1 review citation

The significance of chirality in drug design and development.
Brooks et al. (2011)
15 other articles

2 mentions without citation

Using quantum mechanical approaches to study biological systems.
Merz KM. (2014)
1 more