1US7: Complex of Hsp90 and P50

Name: PDB 1US7: Complex of Hsp90 and P50
Published: 2004-01-15
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Complex of Hsp90 and P50. Determined by X-ray diffraction at 2.3 Å resolution. Released 15 Jan 2004.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: SACCHAROMYCES CEREVISIAE, HOMO SAPIENS
Chains: 2
Atoms: 3,414
Mol. weight: 55.08 kDa
Released: 15 Jan 2004

Explore 1US7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1US7 contains 26 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: 14 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
α-helix	8-9	2
α-helix	10-21	12
α-helix	29-51	23
α-helix	53-58	6
β-strand	64-69	6	1
α-helix	70-72	3
β-strand	74-79	6	1
α-helix	86-88	3
α-helix	89-93	5
α-helix	94	1
α-helix	98-109	12
α-helix	114-120	7
α-helix	123-129	7
β-strand	131-139	9	1
β-strand	145-150	6	1
β-strand	155-160	6	1
α-helix	165-166	2
β-strand	170-177	8	1
α-helix	179-185	7
α-helix	187-197	11
β-strand	205-206	2	1

Chain B: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	149-164	16
α-helix	168-176	9
α-helix	179-181	3
α-helix	184-199	16
α-helix	203-226	24
α-helix	230-232	3
α-helix	234-242	9
α-helix	246-284	39
α-helix	294-300	7
α-helix	302	1
α-helix	317-321	5
α-helix	328-339	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Heat shock protein HSP82	A	protein	214	SACCHAROMYCES CEREVISIAE	P02829 (AlphaFold model)
HSP90 co-chaperone CDC37	B	protein	265	HOMO SAPIENS	Q16543 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1US7_1 HEAT SHOCK PROTEIN HSP82 (chains A)
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEP
DLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQF
GVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDD
QLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVE

Sequence of entity 2 (B), FASTA

>1US7_2 HSP90 CO-CHAPERONE CDC37 (chains B)
MRGSHHHHHHGMASMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQK
YLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRAC
FRQFFTKIKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLD
PVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKE
GEEAGPGDPLLEAVPKTGDEKDVSV

Primary citation

The Mechanism of Hsp90 Regulation by the Protein Kinase-Specific Cochaperone p50(Cdc37). Roe, S.M., Ali, M.M.U., Meyer, P. et al. Cell (2004) 116:87. DOI 10.1016/S0092-8674(03)01027-4 · PubMed

Other PDB entries of the same protein (UniProt P02829 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2IWX 1.5 Å, Analogues of radicicol bound to the ATP-binding site of Hsp90.
2BRC 1.6 Å, Structure of a Hsp90 Inhibitor bound to the N-terminus of Yeast Hsp90.
2WER 1.6 Å, Yeast Hsp90 N-terminal domain LI-IV mutant with Radicicol
3C11 1.6 Å, Yeast Hsp82 N-terminal domain-Geldanamycin complex: effects of mutants 98-99 KS-AA
1ZWH 1.65 Å, Yeast Hsp82 in complex with the novel Hsp90 inhibitor Radester amine
1AH6 1.8 Å, Structure of the tetragonal form of the N-terminal domain of the yeast HSP90 chaperone
1AMW 1.85 Å, ADP binding site in the HSP90 molecular chaperone
2XX2 1.85 Å, Macrolactone Inhibitor bound to HSP90 N-term
1ZW9 1.9 Å, Yeast HSP82 in complex with the Novel HSP90 Inhibitor 8-(6-Bromo-benzo[1,3]dioxol-5-ylsul…
2VW5 1.9 Å, Structure Of The Hsp90 Inhibitor 7-O-carbamoylpremacbecin Bound To The N- Terminus Of…
3C0E 1.9 Å, Yeast Hsp82 N-terminal domain: effects of mutants 98-99 KS-AA
2AKP 1.94 Å, Hsp90 Delta24-N210 mutant

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