1rql Summary


Crystal Structure of Phosponoacetaldehyde Hydrolase Complexed with Magnesium and the Inhibitor Vinyl Sulfonate

The structure was published by Morais, M.C., Zhang, G., Zhang, W., Olsen, D.B., Dunaway-Mariano, D., and Allen, K.N., in 2004 in a paper entitled "X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2003.

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

This PDB entry contains multiple copies of the structure of Phosphonoacetaldehyde Hydrolase.

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 Phosphonoacetaldehyde Hydrolase O31156 (1-264) (PHNX_BACCE)search Bacillus cereussearch 97% 267 96%
B Phosphonoacetaldehyde Hydrolase O31156 (1-264) (PHNX_BACCE)search Bacillus cereussearch 97% 267 96%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O31156 (1 - 264) Phosphonoacetaldehyde Hydrolase Bacillus cereus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (O31156) Phosphonoacetaldehyde hydrolase-likesearch Rossmann foldsearch, Putative phosphatase; domain 2search PF13419: Haloacid dehalogenase-like hydrolasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (O31156) phosphonoacetaldehyde hydrolase activitysearch magnesium ion bindingsearch hydrolase activitysearch metal ion bindingsearch metabolic processsearch organic phosphonate catabolic processsearch

Chain InterPro annotation
A, B Phosphonoacetaldehyde hydrolasesearch HAD hydrolase, subfamily IAsearch Phosphoglycolate phosphatase, domain 2search HAD-like domainsearch