1i0b Summary



The structure was published by Benning, M.M., Shim, H., Raushel, F.M., and Holden, H.M., in 2001 in a paper entitled "High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.3 Å and deposited in 2001.

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

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

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 PHOSPHOTRIESTERASE P0A434 (34-365) (OPD_BREDI)search Brevundimonas diminutasearch 97% 332 99%
B PHOSPHOTRIESTERASE P0A434 (34-365) (OPD_BREDI)search Brevundimonas diminutasearch 97% 332 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0A434 (34 - 365) PHOSPHOTRIESTERASE Brevundimonas diminuta

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P0A434) Phosphotriesterase-likesearch Metal-dependent hydrolasessearch PF02126: Phosphotriesterase familysearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P0A434) hydrolase activity, acting on ester bondssearch zinc ion bindingsearch aryldialkylphosphatase activitysearch hydrolase activitysearch metal ion bindingsearch catabolic processsearch dephosphorylationsearch membranesearch plasma membranesearch

Chain InterPro annotation
A, B Aryldialkylphosphatasesearch Aryldialkylphosphatase, zinc-binding sitesearch