› 5a3y

X-ray diffraction
1.27Å resolution

SAD structure of Thermolysin obtained by multi crystal data collection

Released:
DOI: 10.2210/pdb5a3y/pdb
PDB entry 5a3y coloured by chain, front view.
PDB entry 5a3y coloured by chain, side view.
PDB entry 5a3y coloured by chain, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
MeshAndCollect: an automated multi-crystal data-collection workflow for synchrotron macromolecular crystallography beamlines.
Zander U, Bourenkov G, Popov AN, de Sanctis D, Svensson O, McCarthy AA, Round E, Gordeliy V, Mueller-Dieckmann C, Leonard GA
OpenAccess logo Acta Crystallogr D Biol Crystallogr 71 2328-43 (2015)
PMID: 26527148

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: -|-Leu > -|-Phe.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133580 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermolysin Chain: A
Molecule details ›
Chain: A
Length: 548 amino acids
Theoretical weight: 60.16 KDa
Source organism: Bacillus thermoproteolyticus
UniProt:
  • Canonical: P00800 (Residues: 1-548; Coverage: 100%)
Gene name: npr
Sequence domains:
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand VAL 1 x VAL
Ligand LYS 1 x LYS
Ligand ZN 1 x ZN
Ligand CA 4 x CA
Ligand DMS 1 x DMS
Ligand TMO 2 x TMO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P6122
Unit cell:
a: 92.874Å b: 92.874Å c: 129.167Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.145 0.143 0.166

Quick links

Citations

3 review citations

Best practices for time-resolved serial synchrotron crystallography.
Schulz et al. (2022)
2 more

3 mentions without citation

MeshAndCollect: an automated multi-crystal data-collection workflow for synchrotron macromolecular crystallography beamlines.
Zander et al. (2015)
2 more