1v04 Summary

pdbe.org/1v04
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SERUM PARAOXONASE BY DIRECTED EVOLUTION

The structure was published by Harel, M., Aharoni, A., Gaidukov, L., et al., Silman, I., Sussman, J.L., and Tawfik, D.S., in 2004 in a paper entitled "Structure and Evolution of the Serum Paraoxonase Family of Detoxifying and Anti-Atherosclerotic Enzymes" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2004.

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

The PDB entry contains the structure of SERUM PARAOXONASE/ARYLESTERASE 1.

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 is most likely monomeric.

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 SERUM PARAOXONASE/ARYLESTERASE 1 P27169 (1-353) (PON1_HUMAN)search Homo sapienssearch 99% 355 93%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P27169 (1 - 353) SERUM PARAOXONASE/ARYLESTERASE 1 Homo sapiens, Oryctolagus cuniculus, Mus musculus, Rattus rattus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P27169) Serum paraoxonase/arylesterase 1, PON1search TolB, C-terminal domainsearch PF01731: Arylesterasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P27169) arylesterase activitysearch phospholipid bindingsearch hydrolase activitysearch metal ion bindingsearch protein homodimerization activitysearch aryldialkylphosphatase activitysearch calcium ion bindingsearch phosphatidylcholine metabolic processsearch response to toxic substancesearch response to external stimulussearch positive regulation of bindingsearch dephosphorylationsearch organophosphate catabolic processsearch lipid metabolic processsearch aromatic compound catabolic processsearch positive regulation of cholesterol effluxsearch negative regulation of plasma lipoprotein particle oxidationsearch positive regulation of transporter activitysearch carboxylic acid catabolic processsearch intracellular membrane-bounded organellesearch extracellular spacesearch extracellular regionsearch extracellular vesicular exosomesearch high-density lipoprotein particlesearch blood microparticlesearch spherical high-density lipoprotein particlesearch

Chain InterPro annotation
A Arylesterasesearch Paraoxonase1search Six-bladed beta-propeller, TolB-likesearch