5FM7: RVB1

Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP). Determined by X-ray diffraction at 2.9 Å resolution. Released 20 Jan 2016.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: CHAETOMIUM THERMOPHILUM
Chains: 2
Atoms: 6,540
Mol. weight: 104.78 kDa
Ligands: ADP
Released: 20 Jan 2016

Explore 5FM7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5FM7 contains 42 α-helices and 52 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: 22 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	13-15	3
β-strand	27	1	1
β-strand	33	1	1
α-helix	34	1
β-strand	37	1	2
β-strand	40	1	2
α-helix	44-58	15
β-strand	66-71	6	3
α-helix	77-87	11
β-strand	94-98	5	3
α-helix	99-101	3
α-helix	109-120	12
β-strand	121-132	12	4
β-strand	134-136	3	5
β-strand	161-163	3	5
β-strand	168-170	3	5
α-helix	175-181	7
β-strand	190	1	6
β-strand	191-192	2	5
β-strand	206	1	6
β-strand	207	1	7
α-helix	208-210	3
β-strand	222	1	7
α-helix	223-225	3
β-strand	230-240	11	4
α-helix	241-247	7
α-helix	257-260	4
α-helix	274-289	16
β-strand	293-297	5	4
β-strand	299-303	5	3
α-helix	305-307	3
β-strand	309	1	8
α-helix	310-320	11
α-helix	326	1
β-strand	327-332	6	3
β-strand	336-338	3	9
β-strand	340	1	8
β-strand	346-348	3	9
α-helix	353-356	4
β-strand	359-364	6	3
α-helix	369-383	15
β-strand	387	1	10
α-helix	389-401	13
α-helix	404-409	6
α-helix	411-421	11
β-strand	426	1	10
α-helix	428-437	10
α-helix	441-448	8

Chain B: 20 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	32	1	11
α-helix	38	1
β-strand	39	1	11
α-helix	40	1
β-strand	43	1	12
β-strand	46	1	12
α-helix	50-61	12
β-strand	72-76	5	13
α-helix	83-93	11
β-strand	100-104	5	13
α-helix	105-108	4
α-helix	115-124	10
β-strand	127-145	19	14
β-strand	160-163	4	14
β-strand	168-171	4	14
α-helix	175-183	9
β-strand	190-195	6	14
β-strand	201-206	6	14
β-strand	223	1	14
α-helix	225-227	3
β-strand	232-242	11	14
α-helix	243-249	7
α-helix	253-255	3
α-helix	269-285	17
β-strand	288-292	5	14
β-strand	294-298	5	13
α-helix	300-302	3
β-strand	304	1	15
α-helix	305-314	10
β-strand	322-327	6	13
β-strand	331-333	3	16
β-strand	335	1	15
β-strand	340-342	3	16
α-helix	347-350	4
β-strand	353-357	5	13
α-helix	360-362	3
α-helix	363-375	13
β-strand	381	1	17
α-helix	383-396	14
α-helix	398-414	17
β-strand	420	1	17
α-helix	422-431	10
β-strand	433	1	3
α-helix	435-443	9
β-strand	449	1	18
β-strand	453	1	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RVB1	A	protein	464	CHAETOMIUM THERMOPHILUM	G0RYI5 (AlphaFold model)
RVB2	B	protein	490	CHAETOMIUM THERMOPHILUM	G0RYC2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5FM7_1 RVB1 (chains A)
GAMVQISEVRGNTRDHRTAAHTHIKGLGLNSSGIAEKQAAGFVGQCAAREACGVVVDLIK
AHKMAGRGVLLAGGPGTGKTALALAISQELGTKIPFCPITGSEIYSTEVKKTEVLMENFR
RAIGLRVRETKDVYEGEVTEMTPEEAENPLGGYGKTISTLLIGLKSARGQKKLRLDPSIY
EAIQKERVQVGDVIYIETNTGACKRVGRSDAYATEFDLEAEEYVPIPKGEVHKKKEIVQD
VTLHDLDVANARPQGGQDIISMMGQLMKPKMTEITDKLRMEINKVVQKYINQGVAELIPG
VLFIDEAHMLDIECFTYLNKALESPIAPIVVLASNRGIATIRGADDLKAAHGIPPDFLQR
LLIIPTHPYEPDEIRRIVRIRAQTEGVQLTDAAVDRVAEHGVRISLRYCLQLLAPASILA
RVNGRTQVDVQDIAEAEELFLDARRSANILTSTGESGGLHGFIS

Sequence of entity 2 (B), FASTA

>5FM7_2 RVB2 (chains B)
GAMAAPLVTSVTETKELRGLNLIAAHSHIRGLGVDADTLEPRPSSQGLVGQEKARKAAAV
VLEMIKQGKIAGRAVLIAGPPSTGKTAIAMGMAQSLGQDVPFTTLAASEIFSLEMSKTEA
LTQAFRKSIGVRIKEESEIMEGEVVEIQIDRSVTGGAKQGKLTIKTTDMEAIYDMGSKMI
DAMTKERVMAGDIISIDKSSGKITKLGRSYARSRDYDAMGVDTKFLQCPEGELQKRKEVV
HTVSLHEIDVINSRTQGFLALFSGDTGEIRSEIRDQINTKVAEWKEEGKAEIVPGVLFID
EVHMLDIECFSYINRALESDLAPIVIMASNRGVSRIRGTDYKSPHGLPLDFLDRVVIINT
HPYTPDELRQILSIRAQEEEVDLTPDALALLTKIGQEAGLRYASNLITTSQLIAAKRRAK
QVGVEDVQRSFKLFYDPARSVRFVQESEKRLIGNDGVVDFSYQGAAEAAAPTLPAAAPVD
PVGGEKMDMS

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2

Primary citation

The Combination of X-Ray Crystallography and Cryo-Electron Microscopy Provides Insight Into the Overall Architecture of the Dodecameric Rvb1/Rvb2 Complex. Silva-Martin, N., Dauden, M.I., Glatt, S. et al. PLoS One (2016) 11:46457. DOI 10.1371/JOURNAL.PONE.0146457 · 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
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)
4WVY 3.64 Å, Double-heterohexameric rings of full-length Rvb1(ATP)/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

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