3T0H: Heat shock protein HSP 90-alpha

Structure insights into mechanisms of ATP hydrolysis and the activation of human Hsp90. Determined by X-ray diffraction at 1.2 Å resolution. Released 25 Jan 2012.

Method
X-ray diffraction
Resolution
1.2 Å
Organism
Homo sapiens
Chains
1
Atoms
1,858
Mol. weight
25.66 kDa
Released
25 Jan 2012

Explore 3T0H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3T0H contains 11 α-helices and 8 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: 11 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand18-2141
α-helix22-232
α-helix24-3512
α-helix43-6321
α-helix67-704
β-strand78-8361
β-strand88-9361
α-helix100-1045
α-helix106-1083
α-helix111-12313
α-helix128-1347
α-helix137-1437
β-strand145-15391
β-strand159-16461
β-strand169-17461
β-strand183-19081
α-helix192-1987
α-helix200-21011
β-strand218-22031

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Heat shock protein HSP 90-alphaAprotein228Homo sapiensP07900 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3T0H_1 Heat shock protein HSP 90-alpha (chains A)
DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPS
KLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADI
SMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVIL
HLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAE

Primary citation

Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90. Li, J., Sun, L., Xu, C. et al. Acta Biochim Biophys Sin (Shanghai) (2012) 44:300-306. DOI 10.1093/abbs/gms001 · PubMed

Other PDB entries of the same protein (UniProt P07900 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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