› 5aqe

X-ray diffraction
1.1Å resolution

Cooperative bio-metallic selectivity in a tailored protease enables creation of a C-C cross-coupling Heckase

Released:
DOI: 10.2210/pdb5aqe/pdb
PDB entry 5aqe coloured by chain, front view.
PDB entry 5aqe coloured by chain, side view.
PDB entry 5aqe coloured by chain, top view.
Source organism: Lederbergia lenta
Entry authors: Sharma M, Diaz-Rodriguez A, Offen WA, Palm-Espling ME, Pordea A, Wormald MR, Mcdonough M, Davies GJ, Davis BG

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151551 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin Savinase Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 26.72 KDa
Source organism: Lederbergia lenta
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P29600 (Residues: 1-269; Coverage: 100%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

5 bound ligands:
Ligand VOD 1 x VOD
Ligand SO4 1 x SO4
Ligand CA 1 x CA
Ligand GOL 2 x GOL
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 52.648Å b: 61.246Å c: 74.615Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.077 0.076 0.088
Expression system: Bacillus subtilis

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