Crystal structure of human nuclear receptor sf-1 (nr5a1) bound to pip2 at 2.8 a resolution

Summary for 4QK4

DescriptorSteroidogenic factor 1, Peroxisome proliferator-activated receptor gamma coactivator 1-alpha, (2S)-3-{[(R)-hydroxy{[(1R,2R,3S,4R,5R,6S)-2,3,6-trihydroxy-4,5-bis(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl dihexadecanoate, ... (5 entities in total)
Functional Keywordsnuclear hormone receptor, nr5a1, sf-1 ligand binding domain, regulatory ligands, transcription, transcription regulation, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-biology, partnership for stem cell biology, pip3, pip2, nucleus, nuclear phosphatidylinositol phosphates, transcription factor-hormone complex, stemcell, transcription factor/hormone
Biological sourceHomo sapiens (human)
Cellular locationNucleus  Q13285
Isoform 1: Nucleus. Isoform B4: Nucleus. Isoform B4-8a: Cytoplasm. Isoform B5: Nucleus. Isoform 9: Nucleus  Q9UBK2
Total number of polymer chains2
Total molecular weight30708.59
Joint Center for Structural Genomics (JCSG),Partnership for Stem Cell Biology (STEMCELL) (deposition date: 2014-06-05, release date: 2014-07-30, Last modification date: 2018-03-07)
Primary citation
Blind, R.D.,Sablin, E.P.,Kuchenbecker, K.M.,Chiu, H.J.,Deacon, A.M.,Das, D.,Fletterick, R.J.,Ingraham, H.A.
The signaling phospholipid PIP3 creates a new interaction surface on the nuclear receptor SF-1.
Proc.Natl.Acad.Sci.USA, 111:15054-15059, 2014
PubMed: 25288771 (PDB entries with the same primary citation)
DOI: 10.1073/pnas.1416740111
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.242500 2.3%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-12-02