› 1tht

X-ray diffraction
2.1Å resolution

STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE FROM VIBRIO HARVEYI

Released:
DOI: 10.2210/pdb1tht/pdb
PDB entry 1tht coloured by chain, front view.
PDB entry 1tht coloured by chain, side view.
PDB entry 1tht coloured by chain, top view.
Source organism: Vibrio harveyi
Primary publication:
Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi.
Lawson DM, Derewenda U, Serre L, Ferri S, Szittner R, Wei Y, Meighen EA, Derewenda ZS
Biochemistry 33 9382-8 (1994)
PMID: 8068614

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138699 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 305 amino acids
Theoretical weight: 34.24 KDa
Source organism: Vibrio harveyi
Expression system: Not provided
UniProt:
  • Canonical: P05521 (Residues: 1-305; Coverage: 100%)
Gene name: luxD
Sequence domains: Acyl transferase
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 97.5Å b: 83.8Å c: 47.4Å
α: 90° β: 97.3° γ: 90°
R-values:
R R work R free
0.227 not available not available
Expression system: Not provided

Quick links

Citations

5 review citations

Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases.
Jaeger et al. (1999)
4 more

6 mentions without citation

Thioesterases: a new perspective based on their primary and tertiary structures.
Cantu et al. (2010)
5 more