1E3K: Human Progesteron Receptor Ligand Binding Domain

Human Progesteron Receptor Ligand Binding Domain in complex with the ligand metribolone (R1881). Determined by X-ray diffraction at 2.8 Å resolution. Released 14 Jun 2001.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
4,070
Mol. weight
60.05 kDa
Ligands
R18
Released
14 Jun 2001

Explore 1E3K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1E3K contains 27 α-helices and 8 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 13 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix686-6949
α-helix696-6983
α-helix711-73424
α-helix739-7413
α-helix744-77027
β-strand776-77941
β-strand782-78431
α-helix795-8017
α-helix803-8119
α-helix815-82612
β-strand829-83022
α-helix838-85619
α-helix865-89632
α-helix898-9014
α-helix907-92115
β-strand926-92722
α-helix928-9292
Chain B: 14 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix686-6949
α-helix696-6983
α-helix711-73525
α-helix739-7413
α-helix744-77027
β-strand776-77943
β-strand782-78433
α-helix786-7905
α-helix795-8017
α-helix803-8119
α-helix815-82612
β-strand829-83024
α-helix838-85619
α-helix865-89632
α-helix898-9014
α-helix907-92115
β-strand926-92724
α-helix9281

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Progesterone receptorA, Bprotein258HOMO SAPIENSP06401 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1E3K_1 PROGESTERONE RECEPTOR (chains A, B)
SPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKS
LPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFY
SLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKA
IGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAA
QLPKILAGMVKPLLFHKK

Ligands and cofactors

IDNameFormulaCopies
R18(17BETA)-17-hydroxy-17-methylestra-4,9,11-trien-3-oneC19 H24 O22

Primary citation

Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations. Matias, P.M., Donner, P., Coelho, R. et al. J Biol Chem (2000) 275:26164-26171. DOI 10.1074/jbc.M004571200 · PubMed

Other PDB entries of the same protein (UniProt P06401 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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