Double-heterohexameric rings of full-length Rvb1(ADP)/Rvb2(ADP). Determined by X-ray diffraction at 2.94 Å resolution. Released 18 Feb 2015.
Explore 4WW4 in 3D Show helices and sheets RCSB PDB PDBe
4WW4 contains 43 α-helices and 46 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 27 | 1 | 1 |
| β-strand | 33 | 1 | 1 |
| β-strand | 36-37 | 2 | 2 |
| β-strand | 40-41 | 2 | 2 |
| α-helix | 44-59 | 16 | |
| β-strand | 66-71 | 6 | 3 |
| α-helix | 77-88 | 12 | |
| β-strand | 94-98 | 5 | 3 |
| α-helix | 99-102 | 4 | |
| α-helix | 109-118 | 10 | |
| β-strand | 121-135 | 15 | 4 |
| β-strand | 163-164 | 2 | 4 |
| β-strand | 167-168 | 2 | 4 |
| β-strand | 191-195 | 5 | 4 |
| β-strand | 207 | 1 | 5 |
| α-helix | 208-210 | 3 | |
| β-strand | 222 | 1 | 5 |
| α-helix | 223-225 | 3 | |
| β-strand | 230-240 | 11 | 4 |
| α-helix | 241-248 | 8 | |
| α-helix | 258-261 | 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 | 6 |
| α-helix | 310-321 | 12 | |
| α-helix | 326 | 1 | |
| β-strand | 327-332 | 6 | 3 |
| β-strand | 336-338 | 3 | 7 |
| β-strand | 340 | 1 | 6 |
| β-strand | 346-348 | 3 | 7 |
| α-helix | 353-358 | 6 | |
| β-strand | 359-364 | 6 | 3 |
| α-helix | 365-368 | 4 | |
| α-helix | 369-383 | 15 | |
| β-strand | 387 | 1 | 8 |
| α-helix | 389-401 | 13 | |
| α-helix | 404-408 | 5 | |
| α-helix | 411-421 | 11 | |
| β-strand | 426 | 1 | 8 |
| α-helix | 428-437 | 10 | |
| β-strand | 439 | 1 | 9 |
| α-helix | 441-450 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-15 | 4 | |
| α-helix | 22-24 | 3 | |
| β-strand | 32 | 1 | 10 |
| α-helix | 38 | 1 | |
| β-strand | 39 | 1 | 10 |
| α-helix | 40 | 1 | |
| β-strand | 42-43 | 2 | 11 |
| β-strand | 46-47 | 2 | 11 |
| α-helix | 50-65 | 16 | |
| β-strand | 73-76 | 4 | 9 |
| α-helix | 83-92 | 10 | |
| β-strand | 100-104 | 5 | 9 |
| α-helix | 105-108 | 4 | |
| α-helix | 115-124 | 10 | |
| β-strand | 127-148 | 22 | 12 |
| β-strand | 157-163 | 7 | 12 |
| β-strand | 168-173 | 6 | 12 |
| α-helix | 175-183 | 9 | |
| β-strand | 190-195 | 6 | 12 |
| β-strand | 201-206 | 6 | 12 |
| α-helix | 224-228 | 5 | |
| β-strand | 233-242 | 10 | 12 |
| α-helix | 243-250 | 8 | |
| α-helix | 252-253 | 2 | |
| α-helix | 258-260 | 3 | |
| α-helix | 266-268 | 3 | |
| α-helix | 269-285 | 17 | |
| β-strand | 288-292 | 5 | 12 |
| β-strand | 294-298 | 5 | 9 |
| α-helix | 300-302 | 3 | |
| β-strand | 304 | 1 | 13 |
| α-helix | 305-315 | 11 | |
| β-strand | 322-327 | 6 | 9 |
| β-strand | 331-333 | 3 | 14 |
| β-strand | 335 | 1 | 13 |
| β-strand | 340-342 | 3 | 14 |
| α-helix | 347-352 | 6 | |
| β-strand | 354-357 | 4 | 9 |
| α-helix | 360-362 | 3 | |
| α-helix | 363-376 | 14 | |
| β-strand | 381 | 1 | 15 |
| α-helix | 383-414 | 32 | |
| β-strand | 420 | 1 | 15 |
| α-helix | 422-431 | 10 | |
| α-helix | 435-446 | 12 |
| 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) |
>4WW4_1 RuvB-like 1 (chains A) MVQISEVRGNTRDHRTAAHTHIKGLGLNSSGIAEKQAAGFVGQCAAREACGVVVDLIKAH KMAGRGVLLAGGPGTGKTALALAISQELGTKIPFCPITGSEIYSTEVKKTEVLMENFRRA IGLRVRETKDVYEGEVTEMTPEEAENPLGGYGKTISTLLIGLKSARGQKKLRLDPSIYEA IQKERVQVGDVIYIETNTGACKRVGRSDAYATEFDLEAEEYVPIPKGEVHKKKEIVQDVT LHDLDVANARPQGGQDIISMMGQLMKPKMTEITDKLRMEINKVVQKYINQGVAELIPGVL FIDEAHMLDIECFTYLNKALESPIAPIVVLASNRGIATIRGADDLKAAHGIPPDFLQRLL IIPTHPYEPDEIRRIVRIRAQTEGVQLTDAAVDRVAEHGVRISLRYCLQLLAPASILARV NGRTQVDVQDIAEAEELFLDARRSANILTSTGESGGLHGFIS
>4WW4_2 RuvB-like 2 (chains B) MGSSHHHHHHHHSSGLEVLFQGPGSMAAPLVTSVTETKELRGLNLIAAHSHIRGLGVDAD TLEPRPSSQGLVGQEKARKAAAVVLEMIKQGKIAGRAVLIAGPPSTGKTAIAMGMAQSLG QDVPFTTLAASEIFSLEMSKTEALTQAFRKSIGVRIKEESEIMEGEVVEIQIDRSVTGGA KQGKLTIKTTDMEAIYDMGSKMIDAMTKERVMAGDIISIDKSSGKITKLGRSYARSRDYD AMGVDTKFLQCPEGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIRSEIRDQI NTKVAEWKEEGKAEIVPGVLFIDEVHMLDIECFSYINRALESDLAPIVIMASNRGVSRIR GTDYKSPHGLPLDFLDRVVIINTHPYTPDELRQILSIRAQEEEVDLTPDALALLTKIGQE AGLRYASNLITTSQLIAAKRRAKQVGVEDVQRSFKLFYDPARSVRFVQESEKRLIGNDGV VDFSYQGAAEAAAPTLPAAAPVDPVGGEKMDMS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
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:
MolViewer shows 4WW4 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.