7L7I: Hsp90:FKBP51:p23 closed-state complex

Cryo-EM structure of Hsp90:FKBP51:p23 closed-state complex. Determined by electron microscopy at 3.3 Å resolution. Released 25 Aug 2021.

Method: Electron microscopy
Resolution: 3.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 14,425
Mol. weight: 240.59 kDa
Ligands: ANP
Released: 25 Aug 2021

Explore 7L7I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7L7I contains 81 α-helices and 97 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: 30 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	18-21	4	7
β-strand	23-24	2	8
α-helix	26-35	10
α-helix	43-65	23
α-helix	67-70	4
β-strand	78-83	6	9
β-strand	88-93	6	9
α-helix	100-102	3
α-helix	103-107	5
β-strand	109-110	2	10
α-helix	114-121	8
α-helix	137-140	4
α-helix	141-144	4
β-strand	145-153	9	9
β-strand	159-164	6	9
β-strand	169-174	6	9
β-strand	183-190	8	9
α-helix	195-198	4
α-helix	200-210	11
β-strand	218-222	5	9
β-strand	285-287	3	9
α-helix	296-298	3
α-helix	306-317	12
α-helix	322-323	2
β-strand	325-328	4	11
β-strand	331	1	11
β-strand	337-343	7	11
β-strand	361-365	5	11
β-strand	368-372	5	11
α-helix	380-382	3
β-strand	386-391	6	11
β-strand	396	1	12
β-strand	403	1	12
α-helix	406-427	22
α-helix	431-451	21
α-helix	456-462	7
β-strand	465	1	13
β-strand	466-467	2	14
β-strand	475	1	13
α-helix	477-483	7
β-strand	490-495	6	14
α-helix	499-503	5
α-helix	509-513	5
β-strand	519-521	3	14
α-helix	526-532	7
β-strand	535-536	2	14
β-strand	539-543	5	14
β-strand	546	1	15
α-helix	555-567	13
α-helix	569-578	10
β-strand	580	1	16
β-strand	583	1	16
β-strand	585-588	4	15
β-strand	597-601	5	15
α-helix	608-614	7
α-helix	622-625	4
α-helix	626-628	3
β-strand	632-636	5	15
α-helix	641-652	12
α-helix	657-673	17
α-helix	676-678	3
α-helix	681-696	16

Chain B: 32 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	18-21	4	9
β-strand	23-24	2	10
α-helix	26-35	10
α-helix	41-43	3
α-helix	44-62	19
α-helix	63-65	3
α-helix	67-70	4
β-strand	78-83	6	7
β-strand	88-93	6	7
α-helix	100-106	7
β-strand	109-110	2	8
α-helix	114-119	6
α-helix	137-143	7
β-strand	145-153	9	7
β-strand	159-164	6	7
β-strand	169-174	6	7
β-strand	183-190	8	7
α-helix	192-198	7
α-helix	200-211	12
β-strand	218-223	6	7
β-strand	285-287	3	7
α-helix	296-298	3
α-helix	306-317	12
α-helix	322	1
β-strand	323-332	10	17
β-strand	336-344	9	17
β-strand	361-365	5	17
β-strand	368-371	4	17
α-helix	380-382	3
β-strand	386-391	6	17
α-helix	394-395	2
β-strand	396	1	18
α-helix	397	1
β-strand	403	1	18
α-helix	407-427	21
α-helix	431-451	21
α-helix	456-462	7
β-strand	465-467	3	19
β-strand	474-475	2	19
α-helix	477-483	7
β-strand	490-495	6	19
α-helix	499-504	6
α-helix	506-508	3
α-helix	509-514	6
β-strand	518-521	4	19
α-helix	526-532	7
β-strand	535-536	2	19
β-strand	539-543	5	19
β-strand	546	1	20
α-helix	555-578	24
β-strand	580	1	21
β-strand	583	1	21
β-strand	585-588	4	20
β-strand	597-601	5	20
β-strand	606	1	22
α-helix	608-614	7
α-helix	622-628	7
β-strand	629	1	22
α-helix	630-631	2
β-strand	632-636	5	20
α-helix	641-652	12
α-helix	657-674	18
α-helix	676-678	3
α-helix	681-696	16

Chain C: 18 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	14-17	4
β-strand	23-24	2	1
β-strand	34-39	6	1
β-strand	42	1	2
β-strand	49	1	3
β-strand	52-61	10	1
β-strand	66	1	1
α-helix	71-73	3
β-strand	77-80	4	1
α-helix	88-95	8
β-strand	99	1	2
β-strand	102-107	6	1
α-helix	109-112	4
α-helix	114-116	3
β-strand	118	1	4
β-strand	122	1	4
β-strand	128-138	11	1
β-strand	140-141	2	3
β-strand	148-154	7	3
β-strand	157	1	5
β-strand	167-176	10	3
β-strand	179-189	11	3
α-helix	193-196	4
α-helix	200-205	6
α-helix	206-208	3
β-strand	211	1	5
β-strand	214-219	6	3
α-helix	221-223	3
β-strand	230	1	6
α-helix	231-233	3
β-strand	235	1	6
β-strand	241-251	11	3
α-helix	261-280	20
α-helix	284-299	16
α-helix	306-329	24
α-helix	333-346	14
α-helix	351-363	13
α-helix	367-380	14
α-helix	385-409	25
α-helix	412-419	8

Chain E: 1 helix, 11 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	23
α-helix	3-5	3
β-strand	6-10	5	24
β-strand	14-19	6	24
β-strand	25-32	8	23
β-strand	35-41	7	23
β-strand	48-54	7	23
β-strand	55	1	25
β-strand	59-68	10	24
β-strand	73-79	7	24
β-strand	90	1	25
β-strand	99-101	3	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peptidyl-prolyl cis-trans isomerase FKBP5	C	protein	457	Homo sapiens	Q13451 (AlphaFold model)
Heat shock protein HSP 90-alpha	A, B	protein	732	Homo sapiens	P07900 (AlphaFold model)
Prostaglandin E synthase 3	E	protein	160	Homo sapiens	Q15185 (AlphaFold model)

Sequence of entity 1 (C), FASTA

>7L7I_1 Peptidyl-prolyl cis-trans isomerase FKBP5 (chains C)
MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGK
LSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLP
KIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRM
FDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAE
LIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEM
EYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEA
QLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQD
AKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV

Sequence of entity 2 (A, B), FASTA

>7L7I_2 Heat shock protein HSP 90-alpha (chains A, B)
MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIR
YESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFME
ALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPM
GRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKED
KEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRN
PDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNN
IKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKC
LELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDY
CTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKT
LVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIV
TSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVK
DLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLE
GDDDTSRMEEVD

Sequence of entity 3 (E), FASTA

>7L7I_3 Prostaglandin E synthase 3 (chains E)
MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCID
PNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNF
DRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE

Ligands and cofactors

ID	Name	Formula	Copies
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	2

Primary citation

The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state. Lee, K., Thwin, A.C., Nadel, C.M. et al. Mol Cell (2021) 81:3496. DOI 10.1016/j.molcel.2021.07.023 · PubMed

Other PDB entries of the same protein (UniProt Q13451 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7AOT 0.85 Å, The Fk1 domain of FKBP51 in complex with (2R,5S,12R)-12-cyclohexyl-2-[2-(3,4-dimethoxyphe…
7APW 0.89 Å, The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-(benzo[d]thiazol-6-ylsulfonyl)-5-(…
8R5K 0.89 Å, The Fk1 domain of FKBP51 in complex with Antascomicine B
7APS 0.94 Å, The Fk1 domain of FKBP51 in complex with (2S)-2-((1S,5R,6R)-10-((3,5-dichlorophenyl)sulfo…
3O5Q 0.96 Å, Fk1 domain mutant A19T of FKBP51, crystal form IV, in presence of DMSO
6TX6 0.98 Å, Crystal structure of human FKBP51 FK1 domain A19T mutant in complex with nicotinamide
8CHN 0.99 Å, The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((S)-(3,5-dichlorophenyl)sulfonimi…
3O5P 1.0 Å, Fk1 domain mutant A19T of FKBP51, crystal form IV
4DRQ 1.0 Å, Exploration of Pipecolate Sulfonamides as Binders of the FK506-Binding Proteins 51 and…
5OBK 1.0 Å, The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-((3,5-dichlorophenyl)sulfonyl)-5-(…
8CHP 1.0 Å, The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((S)-(3,5-dichlorophenyl)sulfinyl)…
8CHQ 1.01 Å, The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((S)-3,5-dichloro-N-methylphenylsu…

Browse structure collections

About this viewer

MolViewer shows 7L7I directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.