1a8s Summary



The structure was published by Hofmann, B., Tolzer, S., Pelletier, I., Altenbuchner, J., van Pee, K.H., and Hecht, H.J., in 1998 in a paper entitled "Structural investigation of the cofactor-free chloroperoxidases." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1998.

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

The PDB entry contains the structure of CHLOROPEROXIDASE F. This molecule has the UniProt identifier O31158 (PRXC_PSEFL)search. The sample contained 273 residues which is 100% of the natural sequence. Out of 273 residues 273 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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 CHLOROPEROXIDASE F O31158 (2-274) (PRXC_PSEFL)search Pseudomonas fluorescenssearch 100% 273 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O31158 (2 - 274) CHLOROPEROXIDASE F Pseudomonas fluorescens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (O31158) Haloperoxidasesearch Rossmann foldsearch PF12697: Alpha/beta hydrolase familysearch

Chain ID Molecular function (GO) Biological process (GO)
A (O31158) catalytic activitysearch peroxidase activitysearch oxidoreductase activitysearch chloride peroxidase activitysearch oxidation-reduction processsearch

Chain InterPro annotation
A Alpha/beta hydrolase fold-1search Epoxide hydrolase-likesearch