1qh9 Summary

pdbe.org/1qh9
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ENZYME-PRODUCT COMPLEX OF L-2-HALOACID DEHALOGENASE

A publication describing this structure is not available. The depositing authors are Li, Y.-F.search; Hata, Y.search; Fujii, T.search; Kurihara, T.search; Esaki, N.search

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1999.

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

The PDB entry contains the structure of 2-HALOACID DEHALOGENASE. This molecule has the UniProt identifier Q53464 (HAD_PSEUY)search. The sample contained 232 residues which is 100% of the natural sequence. Out of 232 residues 217 were observed and are deposited in the PDB.

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 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 2-HALOACID DEHALOGENASE Q53464 (1-232) (HAD_PSEUY)search Pseudomonas sp. YLsearch 100% 232 95%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q53464 (1 - 232) 2-HALOACID DEHALOGENASE Pseudomonas sp. YL

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q53464) HAD-relatedsearch Rossmann foldsearch, Putative phosphatase; domain 2search PF00702: haloacid dehalogenase-like hydrolasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (Q53464) hydrolase activitysearch (S)-2-haloacid dehalogenase activitysearch hydrolase activity, acting on acid halide bonds, in C-halide compoundssearch metabolic processsearch

Chain InterPro annotation
A Haloacid dehalogenase, type IIsearch HAD hydrolase, subfamily IAsearch Phosphoglycolate phosphatase, domain 2search HAD-like domainsearch