4WVY: RuvB-like 1

Double-heterohexameric rings of full-length Rvb1(ATP)/Rvb2(apo). Determined by X-ray diffraction at 3.64 Å resolution. Released 18 Feb 2015.

Method: X-ray diffraction
Resolution: 3.64 Å
Organism: Chaetomium thermophilum
Chains: 2
Atoms: 6,456
Mol. weight: 106.9 kDa
Ligands: ATP
Released: 18 Feb 2015

Explore 4WVY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4WVY contains 45 α-helices and 49 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: 25 helices, 25 β-strands

Element	Residues	Length	Sheet
α-helix	13-16	4
α-helix	17-19	3
β-strand	27	1	1
α-helix	32	1
β-strand	33	1	1
α-helix	34	1
β-strand	36-37	2	2
β-strand	40-41	2	2
α-helix	44-58	15
β-strand	66-70	5	3
α-helix	77-88	12
β-strand	94-98	5	3
α-helix	99-102	4
α-helix	111-118	8
β-strand	121-125	5	4
β-strand	127-134	8	5
β-strand	138-139	2	6
β-strand	158-163	6	6
β-strand	168-173	6	6
α-helix	175-183	9
β-strand	192-195	4	5
β-strand	199-202	4	5
α-helix	208-210	3
α-helix	223-225	3
β-strand	230-235	6	5
β-strand	238-240	3	4
α-helix	241-248	8
α-helix	259-261	3
α-helix	274-290	17
β-strand	293-297	5	4
β-strand	299-303	5	3
α-helix	305-307	3
β-strand	309	1	7
α-helix	310-320	11
β-strand	327-332	6	3
β-strand	336-338	3	8
α-helix	339	1
β-strand	340	1	7
β-strand	346-348	3	8
α-helix	353-356	4
β-strand	359-363	5	3
α-helix	365-368	4
α-helix	369-383	15
β-strand	386-387	2	9
α-helix	389-401	13
α-helix	404-409	6
α-helix	411-420	10
β-strand	425-426	2	9
α-helix	428-437	10
α-helix	441-448	8

Chain B: 20 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	32	1	10
β-strand	39	1	10
β-strand	42-43	2	11
β-strand	46-47	2	11
α-helix	50-64	15
β-strand	73-76	4	12
α-helix	83-92	10
β-strand	100-104	5	12
α-helix	105-108	4
α-helix	115-124	10
β-strand	127-143	17	13
β-strand	159-163	5	13
β-strand	168-172	5	13
α-helix	173-174	2
α-helix	175-182	8
β-strand	190-195	6	13
β-strand	201-206	6	13
α-helix	224-227	4
β-strand	232-242	11	13
α-helix	243-250	8
α-helix	252-255	4
α-helix	269-285	17
β-strand	289-292	4	13
β-strand	294-298	5	12
α-helix	300-302	3
β-strand	304	1	14
α-helix	305-315	11
β-strand	322-327	6	12
β-strand	332-333	2	15
α-helix	334	1
β-strand	335	1	14
β-strand	340-341	2	15
α-helix	349-352	4
β-strand	354-357	4	12
α-helix	360-362	3
α-helix	363-376	14
β-strand	381	1	16
α-helix	383-395	13
α-helix	398-414	17
β-strand	420	1	16
α-helix	422-431	10
α-helix	435-446	12
β-strand	450	1	17
β-strand	456	1	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RuvB-like 1	A	protein	462	Chaetomium thermophilum	G0RYI5 (AlphaFold model)
RuvB-like 2	B	protein	513	Chaetomium thermophilum	G0RYC2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4WVY_1 RuvB-like 1 (chains A)
MVQISEVRGNTRDHRTAAHTHIKGLGLNSSGIAEKQAAGFVGQCAAREACGVVVDLIKAH
KMAGRGVLLAGGPGTGKTALALAISQELGTKIPFCPITGSEIYSTEVKKTEVLMENFRRA
IGLRVRETKDVYEGEVTEMTPEEAENPLGGYGKTISTLLIGLKSARGQKKLRLDPSIYEA
IQKERVQVGDVIYIETNTGACKRVGRSDAYATEFDLEAEEYVPIPKGEVHKKKEIVQDVT
LHDLDVANARPQGGQDIISMMGQLMKPKMTEITDKLRMEINKVVQKYINQGVAELIPGVL
FIDEAHMLDIECFTYLNKALESPIAPIVVLASNRGIATIRGADDLKAAHGIPPDFLQRLL
IIPTHPYEPDEIRRIVRIRAQTEGVQLTDAAVDRVAEHGVRISLRYCLQLLAPASILARV
NGRTQVDVQDIAEAEELFLDARRSANILTSTGESGGLHGFIS

Sequence of entity 2 (B), FASTA

>4WVY_2 RuvB-like 2 (chains B)
MGSSHHHHHHHHSSGLEVLFQGPGSMAAPLVTSVTETKELRGLNLIAAHSHIRGLGVDAD
TLEPRPSSQGLVGQEKARKAAAVVLEMIKQGKIAGRAVLIAGPPSTGKTAIAMGMAQSLG
QDVPFTTLAASEIFSLEMSKTEALTQAFRKSIGVRIKEESEIMEGEVVEIQIDRSVTGGA
KQGKLTIKTTDMEAIYDMGSKMIDAMTKERVMAGDIISIDKSSGKITKLGRSYARSRDYD
AMGVDTKFLQCPEGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIRSEIRDQI
NTKVAEWKEEGKAEIVPGVLFIDEVHMLDIECFSYINRALESDLAPIVIMASNRGVSRIR
GTDYKSPHGLPLDFLDRVVIINTHPYTPDELRQILSIRAQEEEVDLTPDALALLTKIGQE
AGLRYASNLITTSQLIAAKRRAKQVGVEDVQRSFKLFYDPARSVRFVQESEKRLIGNDGV
VDFSYQGAAEAAAPTLPAAAPVDPVGGEKMDMS

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1

Primary citation

Structural Basis for Dodecameric Assembly States and Conformational Plasticity of the Full-Length AAA+ ATPases Rvb1Rvb2. Lakomek, K., Stoehr, G., Tosi, A. et al. Structure (2015) 23:483-495. DOI 10.1016/j.str.2014.12.015 · PubMed

Other PDB entries of the same protein (UniProt G0RYI5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8OOP 2.7 Å, CryoEM Structure INO80core Hexasome complex composite model state2
8OO7 2.8 Å, CryoEM Structure INO80core Hexasome complex composite model state1
8OOR 2.87 Å, CryoEM Structure INO80core Hexasome complex Rvb core refinement state2
5FM7 2.9 Å, Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)
8OOC 2.93 Å, CryoEM Structure INO80core Hexasome complex Rvb core refinement state1
4WW4 2.94 Å, Double-heterohexameric rings of full-length Rvb1(ADP)/Rvb2(ADP)
5FM6 3.0 Å, Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(apo)
6FHS 3.75 Å, CryoEM Structure of INO80core
6FML 4.34 Å, CryoEM Structure INO80core Nucleosome complex
8AV6 4.68 Å, CryoEM structure of INO80 core nucleosome complex in closed grappler conformation

Browse structure collections

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