› 2agi

X-ray diffraction
1.14Å resolution

The leupeptin-trypsin covalent complex at 1.14 A resolution

Released:
DOI: 10.2210/pdb2agi/pdb
PDB entry 2agi coloured by chain, front view.
PDB entry 2agi coloured by chain, side view.
PDB entry 2agi coloured by chain, top view.
Source organisms:
Primary publication:
Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates.
Radisky ES, Lee JM, Lu CJ, Koshland DE
Proc Natl Acad Sci U S A 103 6835-40 (2006)
PMID: 16636277

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133349 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease 1 Chain: X
Molecule details ›
Chain: X
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
leupeptin Chain: A
Molecule details ›
Chain: A
Length: 4 amino acids
Theoretical weight: 430 Da
Source organism: Streptomyces roseus
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 61.888Å b: 63.562Å c: 69.102Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.117 0.116 0.138
Expression system: Not provided

Quick links

Citations

2 review citations

The enzymes of β-lactam biosynthesis.
Hamed et al. (2013)
1 more

1 mention without citation

Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates.
Radisky et al. (2006)