› 3qh4

X-ray diffraction
1.75Å resolution

Crystal structure of esterase LipW from Mycobacterium marinum

Released:
DOI: 10.2210/pdb3qh4/pdb
PDB entry 3qh4 coloured by chain, front view.
PDB entry 3qh4 coloured by chain, side view.
PDB entry 3qh4 coloured by chain, top view.
Source organism: Mycobacterium marinum M
Primary publication:
Structural Basis for the Strict Substrate Selectivity of the Mycobacterial Hydrolase LipW.
McKary MG, Abendroth J, Edwards TE, Johnson RJ
Biochemistry 55 7099-7111 (2016)
PMID: 27936614

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109578 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 317 amino acids
Theoretical weight: 33.84 KDa
Source organism: Mycobacterium marinum M
Expression system: Escherichia coli
UniProt:
  • Canonical: B2HLX2 (Residues: 2-312; Coverage: 99%)
Gene names: MMAR_0404, lipW
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P21212
Unit cell:
a: 73.27Å b: 86.99Å c: 46.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.144 0.188
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Distinctive structural motifs co-ordinate the catalytic nucleophile and the residues of the oxyanion hole in the alpha/beta-hydrolase fold enzymes.
Dimitriou et al. (2019)
7 more

7 mentions without citation

Microbial esterases and ester prodrugs: An unlikely marriage for combating antibiotic resistance.
Larsen et al. (2019)
6 more