› 6sxy

X-ray diffraction
2.06Å resolution

STRUCTURE OF S192A-ESTER-HYDROLASE EH3 FROM THE METAGENOME OF MARINE SEDIMENTS AT MILAZZO HARBOR (SICILY, ITALY) COMPLEXED WITH METHYL (2S)-2-PHENYLPROPANOATE

Released:
DOI: 10.2210/pdb6sxy/pdb
PDB entry 6sxy coloured by chain, front view.
PDB entry 6sxy coloured by chain, side view.
PDB entry 6sxy coloured by chain, top view.
Source organism: uncultured bacterium
Primary publication:
Structure and evolutionary trace-assisted screening of a residue swapping the substrate ambiguity and chiral specificity in an esterase.
Cea-Rama I, Coscolín C, Katsonis P, Bargiela R, Golyshin PN, Lichtarge O, Ferrer M, Sanz-Aparicio J
Comput Struct Biotechnol J 19 2307-2317 (2021)
PMID: 33995922

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-104317 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 368 amino acids
Theoretical weight: 40.2 KDa
Source organism: uncultured bacterium
Expression system: Escherichia coli MC1061
UniProt:
  • Canonical: A0A2K8JN75 (Residues: 2-348; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

3 bound ligands:
Ligand PEG 3 x PEG
Ligand LXH 2 x LXH
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: C2
Unit cell:
a: 184.073Å b: 51.707Å c: 70.244Å
α: 90° β: 93.76° γ: 90°
R-values:
R R work R free
0.194 0.192 0.228
Expression system: Escherichia coli MC1061

Quick links

Citations

1 review citation

Genome interpretation using in silico predictors of variant impact.
Katsonis et al. (2022)
3 other articles

1 mention without citation

Structure and evolutionary trace-assisted screening of a residue swapping the substrate ambiguity and chiral specificity in an esterase.
Cea-Rama et al. (2021)