1hbw Summary

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SOLUTION NMR STRUCTURE OF THE DIMERIZATION DOMAIN OF THE YEAST TRANSCRIPTIONAL ACTIVATOR GAL4 (RESIDUES 50-106)

The structure was published by Hidalgo, P., Ansari, A.Z., Schmidt, P., et al., Shin, E.J., Ptashne, M., and Wagner, G., in 2001 in a paper entitled "Recruitment of the Transcriptional Machinery Through Gal11P: Structure and Interactions of the GAL4 Dimerization Domain" (abstract).

The structure was determined using NMR spectroscopy and deposited in 2001.

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

This PDB entry contains multiple copies of the structure of REGULATORY PROTEIN GAL4.

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 REGULATORY PROTEIN GAL4 P04386 (50-106) (GAL4_YEAST)search Saccharomyces cerevisiae S288csearch < 90% 57 100%
B REGULATORY PROTEIN GAL4 P04386 (50-106) (GAL4_YEAST)search Saccharomyces cerevisiae S288csearch < 90% 57 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04386 (50 - 106) REGULATORY PROTEIN GAL4 SACCHAROMYCES CEREVISIAE

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Leucine zipper domainsearch Single alpha-helices involved in coiled-coils or other helix-helix interfacessearch Gal4-like dimerisation domainsearch
Chain InterPro annotation
A, B Gal4 dimerisation domainsearch