› 4kry

X-ray diffraction
2.3Å resolution

Structure of Aes from E. coli in covalent complex with PMS

Released:
DOI: 10.2210/pdb4kry/pdb
PDB entry 4kry coloured by chain, front view.
PDB entry 4kry coloured by chain, side view.
PDB entry 4kry coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural and mutational analyses of Aes, an inhibitor of MalT in Escherichia coli.
Schiefner A, Gerber K, Brosig A, Boos W
Proteins 82 268-77 (2014)
PMID: 23934774

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150087 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl esterase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 333 amino acids
Theoretical weight: 37.91 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P23872 (Residues: 1-319; Coverage: 100%)
Gene names: JW0465, aes, b0476, ybaC
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand PGE 8 x PGE
Ligand IMD 4 x IMD
Ligand 1PE 2 x 1PE
1 modified residue:
Ligand SEB 6 x SEB

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P41
Unit cell:
a: 111.401Å b: 111.401Å c: 282.187Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.209
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Structural basis for dimerization and catalysis of a novel esterase from the GTSAG motif subfamily of the bacterial hormone-sensitive lipase family.
Li et al. (2014)
1 more

2 mentions without citation

Structural insights into the substrate specificity of two esterases from the thermophilic Rhizomucor miehei.
Yang et al. (2015)
1 more