1g88 Summary



The structure was published by Chacko, B.M., Qin, B., Correia, J.J., Lam, S.S., de Caestecker, M.P., and Lin, K., in 2001 in a paper entitled "The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 2000.

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

This PDB entry contains multiple copies of the structure of SMAD4.

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 (285-552) (SMAD4_HUMAN)search Homo sapienssearch < 90% 268 90%
B SMAD4 Q13485 (285-552) (SMAD4_HUMAN)search Homo sapienssearch < 90% 268 90%
C SMAD4 Q13485 (285-552) (SMAD4_HUMAN)search Homo sapienssearch < 90% 268 90%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q13485 (285 - 552) SMAD4 Homo sapiens

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

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

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