1tht Summary

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

The structure was published by Lawson, D.M., Derewenda, U., Serre, L., et al., Wei, Y., Meighen, E.A., and Derewenda, Z.S., in 1994 in a paper entitled "Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1994.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of THIOESTERASE.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A THIOESTERASE P05521 (1-305) (LUXD_VIBHA)search Vibrio harveyisearch 100% 305 96%
B THIOESTERASE P05521 (1-305) (LUXD_VIBHA)search Vibrio harveyisearch 100% 305 96%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05521 (1 - 305) THIOESTERASE Vibrio harveyi

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P05521) Thioesterasessearch Rossmann foldsearch PF02273: Acyl transferasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P05521) transferase activity, transferring acyl groupssearch transferase activity, transferring acyl groups other than amino-acyl groupssearch transferase activitysearch bioluminescencesearch fatty acid metabolic processsearch

Chain InterPro annotation
A, B Acyl transferase, LuxDsearch Alpha/Beta hydrolase foldsearch