› 3vv2

X-ray diffraction
1.83Å resolution

Crystal structure of complex form between S324A-subtilisin and mutant Tkpro

Released:
DOI: 10.2210/pdb3vv2/pdb
PDB entry 3vv2 coloured by chain, front view.
PDB entry 3vv2 coloured by chain, side view.
PDB entry 3vv2 coloured by chain, top view.
Source organism: Thermococcus kodakarensis KOD1
Primary publication:
Accelerated maturation of Tk-subtilisin by a Leu→Pro mutation at the C-terminus of the propeptide, which reduces the binding of the propeptide to Tk-subtilisin.
Uehara R, Ueda Y, You DJ, Koga Y, Kanaya S
FEBS J 280 994-1006 (2013)
PMID: 23237738

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157698 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tk-subtilisin Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 33.9 KDa
Source organism: Thermococcus kodakarensis KOD1
Expression system: Escherichia coli
UniProt:
  • Canonical: P58502 (Residues: 94-422; Coverage: 83%)
Gene name: TK1675
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Tk-subtilisin Chain: B
Molecule details ›
Chain: B
Length: 69 amino acids
Theoretical weight: 7.5 KDa
Source organism: Thermococcus kodakarensis KOD1
Expression system: Escherichia coli
UniProt:
  • Canonical: P58502 (Residues: 25-93; Coverage: 17%)
Gene name: TK1675
Structure domains: Peptidase S8 propeptide/proteinase inhibitor I9

Ligands and Environments

3 bound ligands:
Ligand CA 7 x CA
Ligand CL 1 x CL
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P212121
Unit cell:
a: 65.051Å b: 68.583Å c: 74.054Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.218 0.268
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Progress in Microbial Degradation of Feather Waste.
Li Q. (2019)
4 other articles