› 2sbt

X-ray diffraction
2.8Å resolution

A COMPARISON OF THE THREE-DIMENSIONAL STRUCTURES OF SUBTILISIN BPN AND SUBTILISIN NOVO

Released:
DOI: 10.2210/pdb2sbt/pdb
PDB entry 2sbt coloured by chain, front view.
PDB entry 2sbt coloured by chain, side view.
PDB entry 2sbt coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
A comparison of the three-dimensional structures of subtilisin BPN' and subtilisin novo.
Drenth J, Hol WG, Jansonius JN, Koekoek R
Cold Spring Harb Symp Quant Biol 36 107-16 (1972)
PMID: 4508127

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133530 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin BPN' Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 27.55 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Not provided
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 78%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

1 bound ligand:
Ligand ACN 1 x ACN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 41.2Å b: 78.5Å c: 37.1Å
α: 90° β: 114.6° γ: 90°
Expression system: Not provided

Quick links

Citations

2 review citations

Similarities of protein topologies: evolutionary divergence, functional convergence or principles of folding?
Ptitsyn et al. (1980)
1 more

2 mentions without citation

Multiple structural alignment by secondary structures: algorithm and applications.
Dror et al. (2003)
1 more