1k1v Summary


Solution Structure of the DNA-Binding Domain of MafG

The structure was published by Kusunoki, H., Motohashi, H., Katsuoka, F., Morohashi, A., Yamamoto, M., and Tanaka, T., in 2002 in a paper entitled "Solution structure of the DNA-binding domain of MafG." (abstract).

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

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

The PDB entry contains the structure of MafG. This molecule has the UniProt identifier O54790 (MAFG_MOUSE)search. The sample contained 41 residues which is < 90% of the natural sequence. Out of 41 residues 41 were observed and are deposited in the PDB.

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 MafG O54790 (24-64) (MAFG_MOUSE)search Mus musculussearch < 90% 41 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O54790 (24 - 64) MafG Mus musculus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A A DNA-binding domain in eukaryotic transcription factorssearch Transcription Factor Skn-1; Chain Psearch bZIP Maf transcription factorsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (O54790) sequence-specific DNA binding transcription factor activitysearch DNA bindingsearch nucleussearch regulation of transcription, DNA-templatedsearch

Chain InterPro annotation
A Basic leucine zipper domain, Maf-typesearch Transcription factor, Skn-1-like, DNA-binding domainsearch Transcription factor Mafsearch