2CG9: Hsp90-Sba1 closed chaperone complex

Name: PDB 2CG9: Crystal structure of an Hsp90-Sba1 closed chaperone complex
Published: 2006-04-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Crystal structure of an Hsp90-Sba1 closed chaperone complex. Determined by X-ray diffraction at 3.1 Å resolution. Released 12 Apr 2006.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: SACCHAROMYCES CEREVISIAE
Chains: 4
Atoms: 11,906
Mol. weight: 188.73 kDa
Ligands: ATP
Released: 12 Apr 2006

Explore 2CG9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CG9 contains 61 α-helices and 80 β-strands across 4 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: 29 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
α-helix	12-21	10
α-helix	29-48	20
β-strand	64-69	6	2
α-helix	70-72	3
β-strand	74-79	6	2
α-helix	86-90	5
α-helix	91-93	3
α-helix	102-105	4
α-helix	125-129	5
β-strand	131-139	9	2
β-strand	145-150	6	2
β-strand	155-160	6	2
β-strand	170-177	8	2
α-helix	181-185	5
α-helix	187-197	11
β-strand	205-207	3	2
β-strand	267	1	2
α-helix	281-283	3
α-helix	289-296	8
α-helix	302-303	2
β-strand	305-311	7	3
β-strand	317-323	7	3
β-strand	342-345	4	3
β-strand	348-352	5	3
α-helix	360-362	3
β-strand	366-371	6	3
β-strand	378	1	4
β-strand	382	1	4
α-helix	386-408	23
α-helix	412-431	20
α-helix	436-440	5
β-strand	445	1	5
β-strand	446-447	2	6
β-strand	455	1	5
α-helix	460-463	4
β-strand	470-475	6	6
α-helix	486-488	3
α-helix	489-492	4
β-strand	498-501	4	6
α-helix	504-510	7
α-helix	511-513	3
β-strand	516	1	7
β-strand	519	1	7
β-strand	520-522	3	6
α-helix	540-544	5
α-helix	545-547	3
α-helix	548-556	9
β-strand	565-566	2	8
β-strand	576-579	4	8
α-helix	580-581	2
α-helix	587-593	7
β-strand	612-615	4	8
α-helix	620-630	11
α-helix	643-653	11
α-helix	663-670	8

Chain B: 30 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	2
α-helix	12-21	10
α-helix	29-48	20
β-strand	64-69	6	1
α-helix	70-72	3
β-strand	74-79	6	1
α-helix	86-90	5
α-helix	91-93	3
α-helix	102-105	4
α-helix	125-129	5
β-strand	131-139	9	1
β-strand	145-150	6	1
β-strand	155-160	6	1
β-strand	170-177	8	1
α-helix	181-185	5
α-helix	187-197	11
β-strand	205-208	4	1
β-strand	266-267	2	1
α-helix	281-283	3
α-helix	289-296	8
α-helix	302-303	2
β-strand	307-311	5	9
β-strand	317-322	6	9
β-strand	341-345	5	9
β-strand	348-353	6	9
α-helix	360-362	3
β-strand	366-371	6	9
β-strand	378	1	10
β-strand	382	1	10
α-helix	386-408	23
α-helix	412-431	20
α-helix	436-440	5
β-strand	445	1	11
β-strand	446-447	2	12
β-strand	455	1	11
α-helix	460-463	4
β-strand	470-475	6	12
α-helix	486-488	3
α-helix	489-492	4
β-strand	498-501	4	12
α-helix	504-510	7
α-helix	511-513	3
β-strand	516	1	13
β-strand	519	1	13
β-strand	520-522	3	12
α-helix	533-535	3
α-helix	540-544	5
α-helix	545-547	3
α-helix	548-556	9
β-strand	565-566	2	14
β-strand	576-579	4	14
α-helix	580-581	2
α-helix	587-593	7
β-strand	612-615	4	14
α-helix	620-630	11
α-helix	643-653	11
α-helix	663-670	8

Chains X and Y: 1 helix, 13 β-strands

Element	Residues	Length	Sheet
β-strand	13	1	15
β-strand	17-19	3	16
β-strand	25-29	5	17
β-strand	35-36	2	18
β-strand	42	1	19
β-strand	46-49	4	19
α-helix	51	1
β-strand	52-53	2	18
β-strand	63-64	2	18
β-strand	65	1	15
β-strand	67-70	4	19
β-strand	80-84	5	17
β-strand	91-96	6	17
β-strand	117-119	3	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATP-dependent molecular chaperone HSP82	A, B	protein	677	SACCHAROMYCES CEREVISIAE	P02829 (AlphaFold model)
Co-chaperone protein SBA1	X, Y	protein	134	SACCHAROMYCES CEREVISIAE	P28707 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2CG9_1 ATP-DEPENDENT MOLECULAR CHAPERONE HSP82 (chains A, B)
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEP
DLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQF
GVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDD
QLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDK
KPKLEEVDEEEEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDW
EDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPE
WLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSA
FSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLK
AVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAER
EKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRD
SSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDE
PTSFASRINRLISLGLN

Sequence of entity 2 (X, Y), FASTA

>2CG9_2 CO-CHAPERONE PROTEIN SBA1 (chains X, Y)
SDKVINPQVAWAQRSSTTDPERNYVLITVSIADCDAPELTIKPSYIELKAQSKPHVGDEN
VHHYQLHIDLYKEIIPEKTMHKVANGQHYFLKLYKKDLESEYWPRLTKEKVKYPYIKTDF
DKWVDADEQDEVEA

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2

Primary citation

Crystal Structure of an Hsp90-Nucleotide-P23/Sba1 Closed Chaperone Complex. Ali, M.M.U., Roe, S.M., Vaughan, C. et al. Nature (2006) 440:1013. DOI 10.1038/NATURE04716 · 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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2CG9 is part of these collections:

Protein folding, misfolding and amyloid

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