Cryo-EM structure of Sth1-Arp7-Arp9-Rtt102. Determined by electron microscopy at 4.2 Å resolution. Released 2 Dec 2020.
Explore 6VZG in 3D Show helices and sheets RCSB PDB PDBe
6VZG contains 51 α-helices and 45 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 317-340 | 24 | |
| α-helix | 344-376 | 33 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 34-38 | 5 | 2 |
| β-strand | 46-48 | 3 | 2 |
| α-helix | 51-60 | 10 | |
| β-strand | 66-69 | 4 | 2 |
| β-strand | 71 | 1 | 3 |
| β-strand | 77 | 1 | 3 |
| α-helix | 80-93 | 14 | |
| β-strand | 104-108 | 5 | 1 |
| α-helix | 116-124 | 9 | |
| α-helix | 125-130 | 6 | |
| β-strand | 136-140 | 5 | 1 |
| α-helix | 141-148 | 8 | |
| β-strand | 154-159 | 6 | 4 |
| β-strand | 164-169 | 6 | 4 |
| β-strand | 174 | 1 | 4 |
| β-strand | 180-182 | 3 | 4 |
| α-helix | 186-197 | 12 | |
| α-helix | 198-200 | 3 | |
| α-helix | 215-223 | 9 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-234 | 6 | |
| α-helix | 243-255 | 13 | |
| α-helix | 283-285 | 3 | |
| β-strand | 287-292 | 6 | 5 |
| α-helix | 293-295 | 3 | |
| β-strand | 297-302 | 6 | 5 |
| α-helix | 303-311 | 9 | |
| α-helix | 316-318 | 3 | |
| α-helix | 325-327 | 3 | |
| α-helix | 329-342 | 14 | |
| α-helix | 381-388 | 8 | |
| β-strand | 392-395 | 4 | 4 |
| α-helix | 398-400 | 3 | |
| α-helix | 404-415 | 12 | |
| β-strand | 423-424 | 2 | 4 |
| α-helix | 429-433 | 5 | |
| α-helix | 435-444 | 10 | |
| α-helix | 449-451 | 3 | |
| β-strand | 455 | 1 | 1 |
| α-helix | 457-464 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| β-strand | 10-13 | 4 | 6 |
| β-strand | 18-23 | 6 | 6 |
| β-strand | 26 | 1 | 7 |
| β-strand | 29 | 1 | 7 |
| β-strand | 35-38 | 4 | 6 |
| β-strand | 41-45 | 5 | 8 |
| α-helix | 47-49 | 3 | |
| β-strand | 51-54 | 4 | 8 |
| α-helix | 58-60 | 3 | |
| β-strand | 63-65 | 3 | 8 |
| β-strand | 68-69 | 2 | 9 |
| β-strand | 72-73 | 2 | 9 |
| α-helix | 76-97 | 22 | |
| α-helix | 101-103 | 3 | |
| β-strand | 111-115 | 5 | 6 |
| α-helix | 116 | 1 | |
| α-helix | 121-133 | 13 | |
| β-strand | 140-144 | 5 | 6 |
| α-helix | 145-152 | 8 | |
| β-strand | 159-164 | 6 | 10 |
| β-strand | 169-175 | 7 | 10 |
| β-strand | 178-179 | 2 | 10 |
| β-strand | 185-187 | 3 | 10 |
| α-helix | 191-201 | 11 | |
| α-helix | 207-215 | 9 | |
| α-helix | 276-278 | 3 | |
| β-strand | 282-285 | 4 | 11 |
| α-helix | 290 | 1 | |
| β-strand | 291-294 | 4 | 11 |
| α-helix | 296-299 | 4 | |
| α-helix | 303-317 | 15 | |
| α-helix | 323-330 | 8 | |
| β-strand | 333-336 | 4 | 10 |
| α-helix | 338-341 | 4 | |
| α-helix | 345-357 | 13 | |
| α-helix | 364-373 | 10 | |
| β-strand | 409 | 1 | 10 |
| α-helix | 410-413 | 4 | |
| α-helix | 417-422 | 6 | |
| α-helix | 427-440 | 14 | |
| β-strand | 449 | 1 | 6 |
| α-helix | 451-457 | 7 | |
| α-helix | 458-461 | 4 | |
| α-helix | 462-465 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-9 | 7 | |
| β-strand | 25-30 | 6 | 12 |
| β-strand | 33 | 1 | 13 |
| β-strand | 55 | 1 | 13 |
| β-strand | 60-65 | 6 | 12 |
| β-strand | 88 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin-related protein 7 | L | protein | 477 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q12406 (AlphaFold model) |
| Actin-like protein ARP9 | M | protein | 467 | Saccharomyces cerevisiae | Q05123 (AlphaFold model) |
| Nuclear protein STH1/NPS1 | K | protein | 813 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P32597 (AlphaFold model) |
| Regulator of Ty1 transposition protein 102 | N | protein | 157 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P53330 (AlphaFold model) |
>6VZG_1 Actin-related protein 7 (chains L) MTLNRKCVVIHNGSHRTVAGFSNVELPQCIIPSSYIKRTDEGGEAEFIFGTYNMIDAAAE KRNGDEVYTLVDSQGLPYNWDALEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMAIL ERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVTPIIDGIVVKNAVV RSKFGGDFLDFQVHERLAPLIKEENDMENMADEQKRSTDVWYEASTWIQQFKSTMLQVSE KDLFELERYYKEQADIYAKQQEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFKPLNKTLT LDLKECYQFAEYLFKPQLISDKFSPEDGLGPLMAKSVKKAGASINSMKANTSTNPNGLGT SHINTNVGDNNSTASSSNISPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQYK LTTFANQVMMDRKIQGWLGALTMANLPSWSLGKWYSKEDYETLKRDRKQSQATNATN
>6VZG_2 Actin-like protein ARP9 (chains M) MAPFRQDSILIIYPRSQTTLVQFGLNEETFTVPELEIPTQIYRTTRQDGSYTYHSTNKDN KAELIKPIQNGEIIDISAFTQFLRLIFVSILSDRANKNQDAFEAELSNIPLLLITHHSWS QSDLEIITQYVFESLEINNLIQLPASLAATYSMISLQNCCIIDVGTHHTDIIPIVDYAQL DHLVSSIPMGGQSINDSLKKLLPQWDDDQIESLKKSPIFEVLSDDAKKLSSFDFGNENED EDEGTLNVAEIITSGRDTREVLEERERGQKVKNVKNSDLEFNTFWDEKGNEIKVGKQRFQ GCNNLIKNISNRVGLTLDNIDDINKAKAVWENIIIVGGTTSISGFKEALLGQLLKDHLII EPEEEKSKREEEAKSVLPAATKKKSKFMTNSTAFVPTIEYVQCPTVIKLAKYPDYFPEWK KSGYSEIIFLGAQIVSKQIFTHPKDTFYITREKYNMKGPAALWDVQF
>6VZG_3 Nuclear protein STH1/NPS1 (chains K) MGSSHHHHHHSQDPNSVRLAEELERQQLLEKRKKERNLHLQKINSIIDFIKERQSEQWSR QERCFQFGRLGASLHNQMEKDEQKRIEKTAKQRLAALKSNDEEAYLKLLDQTKDTRITQL LRQTNSFLDSLSEAVRAQQNEAKILHGEEVQPITDEEREKTDYYEVAHRIKEKIDKQPSI LVGGTLKEYQLRGLEWMVSLYNNHLNGILADEMGLGKTIQSISLITYLYEVKKDIGPFLV IVPLSTITNWTLEFEKWAPSLNTIIYKGTPNQRHSLQHQIRVGNFDVLLTTYEYIIKDKS LLSKHDWAHMIIDEGHRMKNAQSKLSFTISHYYRTRNRLILTGTPLQNNLPELWALLNFV LPKIFNSAKTFEDWFNTPFANTGTQEKLELTEEETLLIIRRLHKVLRPFLLRRLKKEVEK DLPDKVEKVIKCKLSGLQQQLYQQMLKHNALFVGAGTEGATKGGIKGLNNKIMQLRKICN HPFVFDEVEGVVNPSRGNSDLLFRVAGKFELLDRVLPKFKASGHRVLMFFQMTQVMDIME DFLRMKDLKYMRLDGSTKTEERTEMLNAFNAPDSDYFCFLLSTRAGGLGLNLQTADTVII FDTDWNPHQDLQAQDRAHRIGQKNEVRILRLITTDSVEEVILERAMQKLDIDGKVIQAGK FDNKSTAEEQEAFLRRLIESETNRDDDDKAELDDDELNDTLARSADEKILFDKIDKERMN QERADAKAQGLRVPPPRLIQLDELPKVFREDIEEHFKKEDSEPLGRIRQKKRVYYDDGLT EEQFLEAVEDDNMSLEDAIKKRREARERRRLRQ
>6VZG_4 Regulator of Ty1 transposition protein 102 (chains N) MDPQTLITKANKVSYYGNPTSKESWRYDWYQPSKVSSNVQQPQQQLGDMENNLEKYPFRY KTWLRNQEDEKNLQRESCEDILDLKEFDRRILKKSLMTSHTKGDTSKATGAPSANQGDEA LSVDDIRGAVGNSEAIPGLSAGVNNDNTKESKDVKMN
| ID | Name | Formula | Copies |
|---|---|---|---|
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
Structural insights into assembly and function of the RSC chromatin remodeling complex. Baker, R.W., Reimer, J.M., Carman, P.J. et al. Nat Struct Mol Biol (2021) 28:71-80. DOI 10.1038/s41594-020-00528-8 · PubMed
Other PDB entries of the same protein (UniProt Q12406 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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