3cp7

X-ray diffraction
1.39Å resolution

Crystal structure of a thermostable serine protease AL20 from extremophilic microoganism

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-112096 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase S1 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 218 amino acids
Theoretical weight: 22.95 KDa
Source organism: Nesterenkonia aethiopica
UniProt:
  • Canonical: D0VWT7 (Residues: 1-218; Coverage: 100%)
Sequence domains: Trypsin
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: R3
Unit cell:
a: 92.26Å b: 92.26Å c: 137.88Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.178 0.199