› 3i77

X-ray diffraction
2.1Å resolution

35/99/170-loops of FXa in SGT

Released:
DOI: 10.2210/pdb3i77/pdb
PDB entry 3i77 coloured by chain, front view.
PDB entry 3i77 coloured by chain, side view.
PDB entry 3i77 coloured by chain, top view.
Source organism: Streptomyces griseus
Primary publication:
Combinatorial enzyme design probes allostery and cooperativity in the trypsin fold.
Page MJ, Di Cera E
J Mol Biol 399 306-19 (2010)
PMID: 20399789

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133479 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypsin Chain: A
Molecule details ›
Chain: A
Length: 230 amino acids
Theoretical weight: 24.1 KDa
Source organism: Streptomyces griseus
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P00775 (Residues: 37-54, 55-57, 58-115, 116-259; Coverage: 98%)
Gene name: sprT
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: I422
Unit cell:
a: 138.351Å b: 138.351Å c: 81.402Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.163 0.195
Expression system: Bacillus subtilis

Quick links

Citations

2 review citations

Proteases as therapeutics.
Craik et al. (2011)
1 more

1 mention without citation

Combinatorial enzyme design probes allostery and cooperativity in the trypsin fold.
Page et al. (2010)