› 4b88

X-ray diffraction
2.05Å resolution

Ancestral (GNCA) Beta-lactamase class A

Released:
DOI: 10.2210/pdb4b88/pdb
PDB entry 4b88 coloured by chain, front view.
PDB entry 4b88 coloured by chain, side view.
PDB entry 4b88 coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian β-lactamases.
Risso VA, Gavira JA, Mejia-Carmona DF, Gaucher EA, Sanchez-Ruiz JM
J Am Chem Soc 135 2899-902 (2013)
PMID: 23394108

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164305 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BETA-LACTAMASE Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 28 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand FMT 3 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: I41
Unit cell:
a: 94.833Å b: 94.833Å c: 95.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.128 0.127 0.166
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

Directed Evolution of Protein Catalysts.
Zeymer et al. (2018)
16 more

4 mentions without citation

De novo active sites for resurrected Precambrian enzymes.
Risso et al. (2017)
3 more