1pyc Summary

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CYP1 (HAP1) DNA-BINDING DOMAIN (RESIDUES 60-100), NMR, 15 STRUCTURES

The structure was published by Timmerman, J., Vuidepot, A.L., Bontems, F., et al., Gervais, M., Shechter, E., and Guiard, B., in 1996 in a paper entitled "1H, 15N resonance assignment and three-dimensional structure of CYP1 (HAP1) DNA-binding domain." (abstract).

The structure was determined using NMR spectroscopy and deposited in 1996.

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

The PDB entry contains the structure of CYP1. This molecule has the UniProt identifier P0CS82 (HAP1_YEASX)search. The sample contained 71 residues which is < 90% of the natural sequence. Out of 71 residues 41 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 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 CYP1 P0CS82 (56-126) (HAP1_YEASX)search Saccharomyces cerevisiaesearch < 90% 71 57%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0CS82 (56 - 126) CYP1 Saccharomyces cerevisiae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Zn2/Cys6 DNA-binding domainsearch CD2-Gal4search Fungal Zn(2)-Cys(6) binuclear cluster domainsearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A (P0CS82) nucleussearch zinc ion bindingsearch sequence-specific DNA binding RNA polymerase II transcription factor activitysearch regulation of transcription, DNA-templatedsearch

Chain InterPro annotation
A Zn(2)-C6 fungal-type DNA-binding domainsearch