› 6sxp

X-ray diffraction
2.15Å resolution

STRUCTURE OF ESTER-HYDROLASE EH3 FROM THE METAGENOME OF MARINE SEDIMENTS AT MILAZZO HARBOR (SICILY, ITALY)

Released:
DOI: 10.2210/pdb6sxp/pdb
PDB entry 6sxp coloured by chain, front view.
PDB entry 6sxp coloured by chain, side view.
PDB entry 6sxp coloured by chain, top view.
Source organism: uncultured bacterium
Primary publication:
Tuning the Properties of Natural Promiscuous Enzymes by Engineering Their Nano-environment.
Giunta CI, Cea-Rama I, Alonso S, Briand ML, Bargiela R, Coscolín C, Corvini PF, Ferrer M, Sanz-Aparicio J, Shahgaldian P
ACS Nano (2020)
PMID: 33306346

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: 40.22 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

2 bound ligands:
Ligand GOL 1 x GOL
Ligand PEG 2 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: C2
Unit cell:
a: 183.296Å b: 51.615Å c: 70.254Å
α: 90° β: 93.86° γ: 90°
R-values:
R R work R free
0.203 0.202 0.228
Expression system: Escherichia coli MC1061

Quick links

Citations

7 citation in other articles

The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity.
Werner et al. (2021)
6 more

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)