7ZTZ: Mutant AR-LBD

Crystal structure of mutant AR-LBD (Y764C) bound to dihydrotestosterone. Determined by X-ray diffraction at 1.4 Å resolution. Released 22 Mar 2023.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Homo sapiens
Chains
1
Atoms
2,161
Mol. weight
29.44 kDa
Ligands
DHT
Released
22 Mar 2023

Explore 7ZTZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7ZTZ contains 13 α-helices and 4 β-strands across 1 chain. 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-helix673-6819
α-helix698-72124
α-helix726-7283
α-helix731-75828
β-strand763-76641
β-strand769-77131
α-helix773-7786
α-helix782-79716
α-helix802-81312
β-strand816-81832
α-helix825-84420
α-helix853-88331
α-helix885-8884
α-helix894-8985
α-helix899-9035
α-helix904-9085
β-strand912-91432

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Androgen receptorAprotein249Homo sapiensP10275 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>7ZTZ_1 Androgen receptor (chains A)
PIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHV
DDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLCFAPDLVFNEYRMHKSRMYSQCVRMRHL
SQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPT
SCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGK
VKPIYFHTQ

Ligands and cofactors

IDNameFormulaCopies
DHT5-alpha-dihydrotestosteroneC19 H30 O21

Water and common crystallization additives (IMD, SO4) are not listed.

Primary citation

A hotspot for posttranslational modifications on the androgen receptor dimer interface drives pathology and anti-androgen resistance. Alegre-Marti, A., Jimenez-Panizo, A., Martinez-Tebar, A. et al. Sci Adv (2023) 9:eade2175-eade2175. DOI 10.1126/sciadv.ade2175 · PubMed

Other PDB entries of the same protein (UniProt P10275 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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