9HPO: Docedameric RuvBL1/RuvBL2

Name: PDB 9HPO: Docedameric RuvBL1/RuvBL2
Published: 2025-12-24
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Docedameric RuvBL1/RuvBL2. Determined by electron microscopy at 3.5 Å resolution. Released 24 Dec 2025.

Method: Electron microscopy
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 12
Atoms: 37,273
Mol. weight: 610.24 kDa
Ligands: ADP
Released: 24 Dec 2025

Explore 9HPO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9HPO contains 239 α-helices and 274 β-strands across 12 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: 22 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	12-15	4
α-helix	16-18	3
β-strand	26	1	1
β-strand	32	1	1
β-strand	35-36	2	2
β-strand	39-40	2	2
α-helix	44-57	14
β-strand	65-69	5	3
α-helix	76-86	11
β-strand	93-97	5	3
α-helix	98-100	3
α-helix	108-117	10
β-strand	120-135	16	4
β-strand	158-159	2	5
β-strand	161-162	2	4
β-strand	170-171	2	5
α-helix	174-182	9
β-strand	189-194	6	4
β-strand	199-201	3	4
β-strand	205-206	2	6
α-helix	207-209	3
β-strand	220-221	2	6
α-helix	222-224	3
β-strand	229-239	11	4
α-helix	242-248	7
α-helix	273-289	17
β-strand	292-296	5	4
β-strand	298-302	5	3
α-helix	304-306	3
β-strand	308	1	7
α-helix	309-320	12
β-strand	326-331	6	3
β-strand	336-337	2	8
α-helix	338	1
β-strand	339	1	7
β-strand	345-346	2	8
α-helix	347-349	3
α-helix	352-355	4
β-strand	358-362	5	3
α-helix	368-382	15
β-strand	385-386	2	9
α-helix	388-400	13
α-helix	403-408	6
α-helix	410-420	11
β-strand	424-425	2	9
α-helix	427-436	10
β-strand	438	1	10
α-helix	440-447	8

Chain B: 22 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	12-15	4
β-strand	26	1	11
β-strand	32	1	11
β-strand	35-36	2	12
β-strand	39-40	2	12
α-helix	43-57	15
β-strand	65-69	5	13
α-helix	76-87	12
β-strand	93-97	5	13
α-helix	98-101	4
α-helix	108-118	11
β-strand	120-131	12	14
β-strand	133-137	5	15
β-strand	158-159	2	16
β-strand	160-162	3	15
β-strand	170-171	2	16
α-helix	174-182	9
β-strand	190-191	2	15
β-strand	192-194	3	14
α-helix	195-197	3
β-strand	199-201	3	14
α-helix	207-209	3
β-strand	229-239	11	14
α-helix	240-246	7
α-helix	275-289	15
β-strand	292-296	5	14
β-strand	298-302	5	13
α-helix	304-306	3
β-strand	308	1	17
α-helix	309-320	12
α-helix	324-325	2
β-strand	326-331	6	13
β-strand	336-337	2	18
α-helix	338	1
β-strand	339	1	17
β-strand	345-346	2	18
α-helix	347-349	3
α-helix	352-355	4
β-strand	358-362	5	13
α-helix	368-382	15
β-strand	386	1	19
α-helix	388-400	13
α-helix	403-408	6
α-helix	410-420	11
β-strand	425	1	19
α-helix	427-434	8
β-strand	437	1	20
α-helix	440-450	11

Chain C: 25 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	12-16	5
β-strand	26	1	21
α-helix	31	1
β-strand	32	1	21
α-helix	33	1
β-strand	35	1	22
β-strand	40	1	22
α-helix	43-57	15
β-strand	66-69	4	23
α-helix	76-86	11
β-strand	93-97	5	23
α-helix	98-100	3
α-helix	108-117	10
β-strand	120-138	19	24
β-strand	158-162	5	24
β-strand	169-171	3	24
α-helix	174-182	9
β-strand	190-194	5	24
β-strand	199-201	3	24
α-helix	207-209	3
β-strand	229-239	11	24
α-helix	240-246	7
α-helix	275-289	15
β-strand	292-296	5	24
β-strand	298-302	5	23
α-helix	304-306	3
α-helix	309-320	12
α-helix	324-325	2
β-strand	326-331	6	23
α-helix	336	1
β-strand	337	1	25
α-helix	338	1
β-strand	345	1	25
α-helix	347-349	3
α-helix	352-355	4
β-strand	359-362	4	23
α-helix	365-367	3
α-helix	368-382	15
β-strand	386	1	26
α-helix	388-400	13
α-helix	403-408	6
α-helix	410-419	10
β-strand	425	1	26
α-helix	427-436	10
β-strand	437-438	2	27
α-helix	440-450	11

Chain D: 17 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	33	1	28
β-strand	39	1	28
β-strand	42	1	29
β-strand	47	1	29
α-helix	50-65	16
β-strand	72-76	5	20
α-helix	83-94	12
β-strand	100-104	5	20
α-helix	105-107	3
α-helix	115-126	12
β-strand	127-135	9	30
β-strand	138	1	31
β-strand	141-144	4	32
β-strand	160-164	5	32
β-strand	169-173	5	32
α-helix	176-184	9
β-strand	233	1	31
β-strand	236-243	8	30
α-helix	244-250	7
α-helix	270-286	17
β-strand	291-293	3	30
β-strand	295-299	5	20
α-helix	301-303	3
β-strand	305	1	33
α-helix	306-316	11
β-strand	323-328	6	20
β-strand	332-334	3	34
β-strand	336	1	33
β-strand	338	1	33
β-strand	341-343	3	34
α-helix	348-352	5
β-strand	354-358	5	20
α-helix	360-362	3
α-helix	364-377	14
β-strand	382	1	35
α-helix	384-396	13
α-helix	399-415	17
β-strand	421	1	35
α-helix	423-430	8
β-strand	433-434	2	3
α-helix	435	1
α-helix	436-446	11

Chain E: 17 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	50-65	16
β-strand	72-77	6	27
α-helix	83-94	12
β-strand	100-104	5	27
α-helix	105-108	4
α-helix	115-126	12
β-strand	127-138	12	36
β-strand	141-144	4	37
β-strand	160-164	5	37
β-strand	169-173	5	37
α-helix	176-184	9
β-strand	192-193	2	38
β-strand	199-200	2	38
β-strand	233-243	11	36
α-helix	244-251	8
α-helix	270-286	17
β-strand	289-293	5	36
β-strand	295-299	5	27
α-helix	301-303	3
β-strand	305	1	39
α-helix	306-315	10
α-helix	321-322	2
β-strand	323-328	6	27
β-strand	332-334	3	40
β-strand	336	1	39
β-strand	341-343	3	40
α-helix	348-352	5
β-strand	354-359	6	27
α-helix	360-362	3
α-helix	364-378	15
β-strand	381-382	2	41
α-helix	384-396	13
α-helix	399-415	17
β-strand	420-421	2	41
α-helix	423-432	10
β-strand	433-434	2	13
α-helix	436-447	12

Chain F: 18 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	30	1	42
β-strand	45	1	42
α-helix	50-65	16
β-strand	73-76	4	10
α-helix	83-94	12
β-strand	100-104	5	10
α-helix	105-107	3
α-helix	115-126	12
β-strand	127-131	5	43
β-strand	134-139	6	44
β-strand	141-142	2	45
β-strand	159	1	46
β-strand	162-164	3	45
β-strand	169-171	3	45
β-strand	174	1	46
α-helix	176-184	9
β-strand	192-193	2	44
β-strand	233-237	5	44
β-strand	240-243	4	43
α-helix	244-251	8
α-helix	271-286	16
β-strand	291-293	3	43
β-strand	295-299	5	10
α-helix	301-303	3
α-helix	306-315	10
α-helix	321-322	2
β-strand	323-328	6	10
β-strand	333-334	2	47
β-strand	341-342	2	47
α-helix	343-345	3
α-helix	348-352	5
β-strand	355-358	4	10
α-helix	359-362	4
α-helix	364-377	14
β-strand	382	1	48
α-helix	384-396	13
α-helix	399-415	17
β-strand	421	1	48
α-helix	423-432	10
β-strand	433-434	2	23
α-helix	436-446	11

Chain G: 22 helices, 25 β-strands

Element	Residues	Length	Sheet
α-helix	16-18	3
β-strand	26	1	49
α-helix	31	1
β-strand	32	1	49
α-helix	33	1
β-strand	35	1	50
β-strand	40	1	50
α-helix	44-57	14
β-strand	65-69	5	51
α-helix	76-87	12
β-strand	93-97	5	51
α-helix	98-101	4
α-helix	108-118	11
β-strand	120-139	20	52
β-strand	158-162	5	52
β-strand	170-171	2	52
α-helix	174-182	9
β-strand	189-194	6	52
β-strand	199-201	3	52
β-strand	205-206	2	53
α-helix	207-209	3
β-strand	220-221	2	53
α-helix	222-224	3
β-strand	229-239	11	52
α-helix	240-248	9
α-helix	273-289	17
β-strand	292-296	5	52
β-strand	298-302	5	51
α-helix	304-306	3
β-strand	308	1	54
α-helix	309-320	12
β-strand	326-331	6	51
β-strand	336-337	2	55
α-helix	338	1
β-strand	339	1	54
β-strand	345-346	2	55
α-helix	347-349	3
α-helix	352-355	4
β-strand	358-362	5	51
α-helix	368-381	14
β-strand	386	1	56
α-helix	388-400	13
α-helix	403-419	17
β-strand	425	1	56
α-helix	427-436	10
β-strand	437-438	2	57
α-helix	440-447	8

Chain H: 22 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	12-15	4
β-strand	26	1	58
β-strand	32	1	58
β-strand	35-36	2	59
β-strand	39-40	2	59
α-helix	43-57	15
β-strand	65-69	5	60
α-helix	76-87	12
β-strand	93-97	5	60
α-helix	98-101	4
α-helix	108-118	11
β-strand	120-137	18	61
β-strand	158-162	5	61
β-strand	168-171	4	61
α-helix	174-182	9
β-strand	190-194	5	61
β-strand	199-201	3	61
α-helix	207-209	3
β-strand	229-239	11	61
α-helix	240-246	7
α-helix	275-289	15
β-strand	292-296	5	61
β-strand	298-302	5	60
α-helix	304-306	3
β-strand	308	1	62
α-helix	309-320	12
α-helix	324-325	2
β-strand	326-331	6	60
β-strand	336-337	2	63
α-helix	338	1
β-strand	339	1	62
β-strand	345-346	2	63
α-helix	347-349	3
α-helix	352-355	4
β-strand	358-362	5	60
α-helix	365-367	3
α-helix	368-382	15
β-strand	386	1	64
α-helix	388-400	13
α-helix	403-420	18
β-strand	425	1	64
α-helix	426	1
α-helix	427-434	8
β-strand	437	1	65
α-helix	440-450	11

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RuvB-like 1	A, B, C, G, H, I	protein	451	Homo sapiens	Q9Y265 (AlphaFold model)
RuvB-like 2	D, E, F, J, K, L	protein	463	Homo sapiens	Q9Y230 (AlphaFold model)

Sequence of entity 1 (A, B, C, G, H, I), FASTA

>9HPO_1 RuvB-like 1 (chains A, B, C, G, H, I)
MKIEEVKSTTKTQRIASHSHVKGLGLDESGLAKQAASGLVGQENAREACGVIVELIKSKK
MAGRAVLLAGPPGTGKTALALAIAQELGSKVPFCPMVGSEVYSTEIKKTEVLMENFRRAI
GLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIGLKTAKGTKQLKLDPSIFESL
QKERVEAGDVIYIEANSGAVKRQGRCDTYATEFDLEAEEYVPLPKGDVHKKKEIIQDVTL
HDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEINKVVNKYIDQGIAELVPGVLF
VDEVHMLDIECFTYLHRALESSIAPIVIFASNRGNCVIRGTEDITSPHGIPLDLLDRVMI
IRTMLYTPQEMKQIIKIRAQTEGINISEEALNHLGEIGTKTTLRYSVQLLTPANLLAKIN
GKDSIEKEHVEEISELFYDAKSSAKILADQQ

Sequence of entity 2 (D, E, F, J, K, L), FASTA

>9HPO_2 RuvB-like 2 (chains D, E, F, J, K, L)
MATVTATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQASQGMVGQLAARRAAGVVL
EMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTAIAGSEIFSLEMSKTEALT
QAFRRSIGVRIKEETEIIEGEVVEIQIDRPATGTGSKVGKLTLKTTEMETIYDLGTKMIE
SLTKDKVQAGDVITIDKATGKISKLGRSFTRARDYDAMGSQTKFVQCPDGELQKRKEVVH
TVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDE
VHMLDIESFSFLNRALESDMAPVLIMATNRGITRIRGTSYQSPHGIPIDLLDRLLIVSTT
PYSEKDTKQILRIRCEEEDVEMSEDAYTVLTRIGLETSLRYAIQLITAASLVCRKRKGTE
VQVDDIKRVYSLFLDESRSTQYMKEYQDAFLFNELKGETMDTS

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	12

Primary citation

An integrative structural biology approach reveals the dynamic organization of the R2SP quaternary chaperone complex. Santo, P.E., Chagot, M.E., Gizardin-Fredon, H. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-69157-x · PubMed

Other PDB entries of the same protein (UniProt Q9Y265 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2C9O 2.2 Å, 3D Structure of the human RuvB-like helicase RuvBL1
8QR1 2.4 Å, Cryo-EM structure of the human Tip60 complex
9EMA 2.4 Å, RUVBL1/2 in complex with ATP and CB-6644 inhibitor
6K0R 2.5 Å, Ruvbl1-Ruvbl2 with truncated domain II in complex with phosphorylated Cordycepin
9C57 2.75 Å, Reconstituted P400 Subcomplex of the human TIP60 complex
2XSZ 3.0 Å, The dodecameric human RuvBL1:RuvBL2 complex with truncated domains II
9CAE 3.07 Å, Cryo-EM structure of the reconstituted RuvBL lobe of the human TIP60 complex (composite…
7ZI4 3.2 Å, Cryo-EM structure of the human INO80 complex bound to a WT nucleosome
8X15 3.2 Å, Structure of nucleosome-bound SRCAP-C in the apo state
8X19 3.2 Å, Structure of nucleosome-bound SRCAP-C in the ADP-BeFx-bound state
8X1C 3.2 Å, Structure of nucleosome-bound SRCAP-C in the ADP-bound state
8XVT 3.2 Å, The core subcomplex of human NuA4/TIP60 complex

Browse structure collections

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