› 2xtt

X-ray diffraction
0.93Å resolution

Bovine trypsin in complex with evolutionary enhanced Schistocerca gregaria protease inhibitor 1 (SGPI-1-P02)

Released:
DOI: 10.2210/pdb2xtt/pdb
PDB entry 2xtt coloured by chain, front view.
PDB entry 2xtt coloured by chain, side view.
PDB entry 2xtt coloured by chain, top view.
Source organisms:
Primary publication:
The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action.
Wahlgren WY, Pál G, Kardos J, Porrogi P, Szenthe B, Patthy A, Gráf L, Katona G
J Biol Chem 286 3587-96 (2011)
PMID: 21097875

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129208 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protease inhibitor SGPI-1 Chain: A
Molecule details ›
Chain: A
Length: 36 amino acids
Theoretical weight: 3.93 KDa
Source organism: Schistocerca gregaria
Expression system: Not provided
UniProt:
  • Canonical: O46162 (Residues: 20-54; Coverage: 48%)
Sequence domains: Pacifastin inhibitor (LCMII)
Serine protease 1 Chain: B
Molecule details ›
Chain: B
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 ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 36.91Å b: 63.61Å c: 43.87Å
α: 90° β: 93.85° γ: 90°
R-values:
R R work R free
0.117 not available 0.14
Expression system: Not provided

Quick links

Citations

12 citation in other articles

Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad.
Buller et al. (2013)
11 more

3 mentions without citation

Monospecific inhibitors show that both mannan-binding lectin-associated serine protease-1 (MASP-1) and -2 Are essential for lectin pathway activation and reveal structural plasticity of MASP-2.
Héja et al. (2012)
2 more