› 3ljj

X-ray diffraction
1.55Å resolution

Bovine trypsin in complex with UB-THR 10

Released:
DOI: 10.2210/pdb3ljj/pdb
PDB entry 3ljj coloured by chain, front view.
PDB entry 3ljj coloured by chain, side view.
PDB entry 3ljj coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Congeneric but still distinct: how closely related trypsin ligands exhibit different thermodynamic and structural properties.
Brandt T, Holzmann N, Muley L, Khayat M, Wegscheid-Gerlach C, Baum B, Heine A, Hangauer D, Klebe G
J Mol Biol 405 1170-87 (2011)
PMID: 21111747

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

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
Expression system: Escherichia coli
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

3 bound ligands:
Ligand 10U 1 x 10U
Ligand CA 1 x CA
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 61.6Å b: 63.7Å c: 69.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.253 not available
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Entropy-enthalpy compensation: role and ramifications in biomolecular ligand recognition and design.
Chodera et al. (2013)
5 more

2 mentions without citation

Be on Target: Strategies of Targeting Alternative and Lectin Pathway Components in Complement-Mediated Diseases.
Dobó et al. (2018)
1 more