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CRYSTAL STRUCTURE OF THE SMAD4 TUMOR SUPPRESSOR C-TERMINAL DOMAIN

The structure was published by Shi, Y., Hata, A., Lo, R.S., Massague, J., and Pavletich, N.P., in 1997 in a paper entitled "A structural basis for mutational inactivation of the tumour suppressor Smad4." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1997.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of SMAD4. This molecule has the UniProt identifier Q13485 (SMAD4_HUMAN)search. The sample contained 234 residues which is < 90% of the natural sequence. Out of 234 residues 190 were observed and are deposited in the PDB.

The molecule most likely forms homotrimers.

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 SMAD4 Q13485 (319-552) (SMAD4_HUMAN)search Homo sapienssearch < 90% 234 81%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q13485 (319 - 552) SMAD4 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A SMAD domainsearch Tumour Suppressor Smad4search MH2 domainsearch

Chain ID Cellular component (GO) Biological process (GO)
A (Q13485) intracellularsearch regulation of transcription, DNA-templatedsearch

Chain InterPro annotation
A SMAD domain, Dwarfin-typesearch SMAD/FHA domainsearch Dwarfinsearch SMAD domain-likesearch