› 4ia5

X-ray diffraction
2.22Å resolution

Hydratase from Lactobacillus acidophilus - SeMet derivative (apo LAH)

Released:
DOI: 10.2210/pdb4ia5/pdb
PDB entry 4ia5 coloured by chain, front view.
PDB entry 4ia5 coloured by chain, side view.
PDB entry 4ia5 coloured by chain, top view.
Source organism: Lactobacillus acidophilus NCFM
Primary publication:
Crystal structure analysis of a fatty acid double-bond hydratase from Lactobacillus acidophilus.
Volkov A, Khoshnevis S, Neumann P, Herrfurth C, Wohlwend D, Ficner R, Feussner I
Acta Crystallogr D Biol Crystallogr 69 648-57 (2013)
PMID: 23519674

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177110 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myosin-crossreactive antigen Chains: A, B
Molecule details ›
Chains: A, B
Length: 591 amino acids
Theoretical weight: 68.54 KDa
Source organism: Lactobacillus acidophilus NCFM
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5FL96 (Residues: 1-591; Coverage: 100%)
Gene name: LBA0649
Sequence domains: MCRA family
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand MES 2 x MES
Ligand K 2 x K
Ligand MPD 5 x MPD
Ligand NA 1 x NA
Ligand PO4 1 x PO4
Ligand GOL 3 x GOL
1 modified residue:
Ligand MSE 36 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21212
Unit cell:
a: 168.75Å b: 78.97Å c: 108.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.258
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Fatty Acids and their Derivatives as Renewable Platform Molecules for the Chemical Industry.
Biermann et al. (2021)
5 more

1 mention without citation

Structure-Based Mechanism of Oleate Hydratase from Elizabethkingia meningoseptica.
Engleder et al. (2015)