3hc5 Summary

pdbe.org/3hc5
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FXR with SRC1 and GSK826

The structure was published by Akwabi-Ameyaw, A., Bass, J.Y., Caldwell, R.D., et al., Todd, D., Williams, S.P., and Bruce Wisely, G., in 2009 in a paper entitled "FXR agonist activity of conformationally constrained analogs of GW 4064." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2009.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Bile acid receptor and Nuclear receptor coactivator 1.

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 most likely forms heterodimers.

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 Bile acid receptor Q96RI1 (257-486) (NR1H4_HUMAN)search Homo sapienssearch < 90% 232 98%
B Nuclear receptor coactivator 1 Q15788 (741-761) (NCOA1_HUMAN)search Homo sapienssearch < 90% 21 52%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
Q96RI1 (257 - 486) Bile acid receptor Homo sapiens
Q15788 (741 - 761) Nuclear receptor coactivator 1

Chain Structural classification (CATH) Sequence family (Pfam)
A Retinoid X Receptorsearch Ligand-binding domain of nuclear hormone receptorsearch
B

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (Q96RI1) regulation of transcription, DNA-templatedsearch steroid hormone mediated signaling pathwaysearch steroid hormone receptor activitysearch sequence-specific DNA binding transcription factor activitysearch DNA bindingsearch nucleussearch

Chain InterPro annotation
A Nuclear hormone receptor, ligand-binding, coresearch Steroid hormone receptorsearch Nuclear hormone receptor, ligand-bindingsearch
B