2VW5: Hsp90 Inhibitor 7-O-carbamoylpremacbecin

Structure Of The Hsp90 Inhibitor 7-O-carbamoylpremacbecin Bound To The N- Terminus Of Yeast Hsp90. Determined by X-ray diffraction at 1.9 Å resolution. Released 2 Sept 2008.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: SACCHAROMYCES CEREVISIAE
Chains: 4
Atoms: 7,518
Mol. weight: 99.71 kDa
Ligands: BC6
Released: 2 Sept 2008

Explore 2VW5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2VW5 contains 51 α-helices and 32 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: 13 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	4-7	4	1
α-helix	8-9	2
α-helix	10-22	13
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	86-92	7
α-helix	101-109	9
α-helix	114-120	7
α-helix	123-129	7
β-strand	131-139	9	1
β-strand	146-150	5	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	205-207	3	1

Chain B: 12 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	2
α-helix	8-9	2
α-helix	10-22	13
α-helix	29-51	23
α-helix	53-58	6
β-strand	64-69	6	2
α-helix	70-72	3
β-strand	74-79	6	2
α-helix	86-92	7
α-helix	101-109	9
α-helix	114-120	7
α-helix	123-129	7
β-strand	131-139	9	2
β-strand	146-150	5	2
β-strand	155-160	6	2
α-helix	165-167	3
β-strand	170-177	8	2
α-helix	179-185	7
α-helix	187-197	11
β-strand	205-207	3	2

Chain C: 13 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	4-7	4	3
α-helix	8-9	2
α-helix	10-22	13
α-helix	29-49	21
α-helix	53-58	6
β-strand	64-69	6	3
α-helix	70-72	3
β-strand	74-79	6	3
α-helix	86-92	7
α-helix	101-110	10
α-helix	114-120	7
α-helix	123-129	7
β-strand	131-139	9	3
β-strand	146-150	5	3
β-strand	155-160	6	3
α-helix	165-167	3
β-strand	170-177	8	3
α-helix	179-185	7
α-helix	187-197	11
β-strand	205-207	3	3

Chain D: 13 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	4-7	4	4
α-helix	8-9	2
α-helix	10-20	11
α-helix	29-51	23
α-helix	53-56	4
β-strand	64-69	6	4
α-helix	70-72	3
β-strand	74-79	6	4
α-helix	86-92	7
α-helix	101-110	10
α-helix	114-120	7
α-helix	123-129	7
β-strand	131-139	9	4
β-strand	146-150	5	4
β-strand	155-160	6	4
α-helix	165-167	3
β-strand	170-177	8	4
α-helix	182-185	4
α-helix	187-197	11
β-strand	205-207	3	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATP-dependent molecular chaperone HSP82	A, B, C, D	protein	214	SACCHAROMYCES CEREVISIAE	P02829 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>2VW5_1 ATP-DEPENDENT MOLECULAR CHAPERONE HSP82 (chains A, B, C, D)
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEP
DLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQF
GVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDD
QLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVE

Ligands and cofactors

ID	Name	Formula	Copies
BC6	(4E,8S,9R,10E,12S,13R,14S,16R)-13,20-dihydroxy-14-methoxy-4,8,10,12,16-pentamet…	C28 H42 N2 O6	4

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

Primary citation

Optimizing Natural Products by Biosynthetic Engineering: Discovery of Nonquinone Hsp90 Inhibitors. Zhang, M.Q., Gaisser, S., Nur-E-Alam, M. et al. J Med Chem (2008) 51:5494. DOI 10.1021/JM8006068 · 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…
3C0E 1.9 Å, Yeast Hsp82 N-terminal domain: effects of mutants 98-99 KS-AA
2AKP 1.94 Å, Hsp90 Delta24-N210 mutant
2YGE 1.96 Å, E88G-N92L Mutant of N-Term HSP90 complexed with Geldanamycin

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