4ixt Summary

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Structure of a 37-fold mutant of halohydrin dehalogenase (HheC) bound to ethyl (R)-4-cyano-3-hydroxybutyrate

The structure was published by Schallmey, M., Floor, R.J., Hauer, B., et al., Wijma, H.J., Dijkstra, B.W., and Janssen, D.B., in 2013 in a paper entitled "Biocatalytic and structural properties of a highly engineered halohydrin dehalogenase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.49 Å and deposited in 2013.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Halohydrin dehalogenase.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotetramers.

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 Halohydrin dehalogenase Q93D82 (1-254) (Q93D82_RHIRD)search Agrobacterium tumefacienssearch 100% 254 98%
B Halohydrin dehalogenase Q93D82 (1-254) (Q93D82_RHIRD)search Agrobacterium tumefacienssearch 100% 254 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q93D82 (1 - 254) Halohydrin dehalogenase Agrobacterium tumefaciens

Chain Sequence family (Pfam)
A, B (Q93D82) PF13561: Enoyl-(Acyl carrier protein) reductasesearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (Q93D82) metabolic processsearch oxidoreductase activitysearch metal ion bindingsearch

Chain InterPro annotation
A, B Glucose/ribitol dehydrogenasesearch NAD(P)-binding domainsearch