Brand  (β version)

PDB ID: 4DMA

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Ligands
Code Name Style Show Link
0L8 2'-bromo-6'-(furan-3-yl)-4'-(hydroxymethyl)biphenyl-4-ol PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 4DMA   PDBj   RCSB PDB   PDBe
Header : TRANSCRIPTION/protein binding/agonist
Title : Crystal structure of ERa LBD in complex with RU100132
Release Data : 2012-03-07
Compound :
mol_id molecule chains synonym
1 Estrogen receptor A,B ER, ER-alpha, Estradiol receptor, Nuclear receptor subfamily 3 group A member 1
fragment: unp residues 303-549
mutation: C530A
mol_id molecule chains synonym
2 Nuclear receptor coactivator 1 E,F NCoA-1, Nuclear receptor coactivator protein 1, mNRC-1, Steroid receptor coactivator 1, SRC-1
ec: 2.3.1.48
fragment: unp residues 690-704
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: ESR1, ESR, NR3A1
expression_system_vector_type: plasmid
expression_system_plasmid: pET15b
mol_id organism_scientific organism_common
2 Mus musculus  (taxid:10090) Mouse
synthetic: yes
Authors : Osz, J., Brelivet, Y., Peluso-Iltis, C., Cura, V., Eiler, S., Ruff, M., Bourguet, W., Rochel, N., Moras, D.
Keywords : transcription, nuclear receptor, ER, estrogen receptor, alpha helical sandwich, transcription factor, estradiol, TRANSCRIPTION-protein binding-agonist complex
Exp. method : X-RAY DIFFRACTION ( 2.3 Å )
Citation :

Structural basis for a molecular allosteric control mechanism of cofactor binding to nuclear receptors.

Osz, J.,Brelivet, Y.,Peluso-Iltis, C.  et al.
(2012)  Proc.Natl.Acad.Sci.USA  109 : E588 - E594

PubMed: 22355136
DOI: 10.1073/pnas.1118192109

Cleaved thioredoxin fusion protein enables the crystallization of poorly soluble ERalpha in complex with synthetic ligands.

Cura, V.,Gangloff, M.,Eiler, S.  et al.
(2008)  Acta Crystallogr.,Sect.F  64 : 54 - 57

PubMed: 18097104
DOI: 10.1107/S1744309107066444

Reaction

Chain : A, B
UniProt : P03372 (ESR1_HUMAN)
Reaction : -
Chain : E, F
UniProt : P70365 (NCOA1_MOUSE)
Reaction: EC: Evidence:
Physiological Direction:
acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- lysyl-[protein] 2.3.1.48 -
-