› 1btz

X-ray diffraction
2Å resolution

Episelection: novel KI ~nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface

Released:
DOI: 10.2210/pdb1btz/pdb
PDB entry 1btz coloured by chain, front view.
PDB entry 1btz coloured by chain, side view.
PDB entry 1btz coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface.
Katz BA, Finer-Moore J, Mortezaei R, Rich DH, Stroud RM
Biochemistry 34 8264-80 (1995)
PMID: 7599119

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)
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
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

2 bound ligands:
Ligand 0ZY 1 x 0ZY
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 54.84Å b: 58.61Å c: 67.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.134 0.134 not available

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Citations

3 review citations

Drug discovery by dynamic combinatorial libraries.
Ramström et al. (2002)
2 more

5 mentions without citation

Improvement in protein functional site prediction by distinguishing structural and functional constraints on protein family evolution using computational design.
Cheng et al. (2005)
4 more