Structure of the full-length yeast Arp7-Arp9 Heterodimer. Determined by X-ray diffraction at 3.1 Å resolution. Released 26 Feb 2014.
Explore 3WEE in 3D Show helices and sheets RCSB PDB PDBe
3WEE contains 45 α-helices and 42 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 | 10-14 | 5 | 1 |
| β-strand | 18-23 | 6 | 1 |
| β-strand | 35-38 | 4 | 1 |
| β-strand | 41-45 | 5 | 2 |
| β-strand | 51-54 | 4 | 2 |
| β-strand | 63-65 | 3 | 2 |
| β-strand | 68-69 | 2 | 3 |
| β-strand | 72-73 | 2 | 3 |
| α-helix | 76-91 | 16 | |
| β-strand | 111-115 | 5 | 1 |
| α-helix | 121-133 | 13 | |
| β-strand | 139-144 | 6 | 1 |
| α-helix | 145-152 | 8 | |
| β-strand | 159-164 | 6 | 4 |
| β-strand | 169-175 | 7 | 4 |
| β-strand | 178-179 | 2 | 4 |
| β-strand | 185-187 | 3 | 4 |
| α-helix | 191-201 | 11 | |
| α-helix | 207-214 | 8 | |
| β-strand | 220 | 1 | 5 |
| α-helix | 221-223 | 3 | |
| α-helix | 224-228 | 5 | |
| β-strand | 251-254 | 4 | 6 |
| β-strand | 282-285 | 4 | 6 |
| β-strand | 290-294 | 5 | 6 |
| α-helix | 296-299 | 4 | |
| α-helix | 303-318 | 16 | |
| α-helix | 323-331 | 9 | |
| β-strand | 333-336 | 4 | 4 |
| α-helix | 338-341 | 4 | |
| β-strand | 343 | 1 | 5 |
| α-helix | 345-357 | 13 | |
| α-helix | 363-374 | 12 | |
| α-helix | 379-386 | 8 | |
| α-helix | 389-390 | 2 | |
| α-helix | 396-399 | 4 | |
| β-strand | 400 | 1 | 7 |
| β-strand | 409 | 1 | 4 |
| α-helix | 410-412 | 3 | |
| α-helix | 424-440 | 17 | |
| β-strand | 449-450 | 2 | 1 |
| α-helix | 451-457 | 7 | |
| α-helix | 458-464 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 8 |
| β-strand | 16-21 | 6 | 8 |
| β-strand | 29-32 | 4 | 8 |
| β-strand | 35-39 | 5 | 9 |
| β-strand | 45-48 | 4 | 9 |
| α-helix | 51-60 | 10 | |
| β-strand | 65-68 | 4 | 9 |
| β-strand | 71 | 1 | 10 |
| β-strand | 77 | 1 | 10 |
| α-helix | 80-89 | 10 | |
| α-helix | 90-94 | 5 | |
| β-strand | 104-108 | 5 | 8 |
| α-helix | 115-116 | 2 | |
| α-helix | 117-124 | 8 | |
| α-helix | 125-130 | 6 | |
| β-strand | 136-140 | 5 | 8 |
| α-helix | 141-148 | 8 | |
| β-strand | 154-159 | 6 | 11 |
| β-strand | 164-169 | 6 | 11 |
| β-strand | 170 | 1 | 12 |
| β-strand | 173 | 1 | 12 |
| α-helix | 176-178 | 3 | |
| β-strand | 180-181 | 2 | 11 |
| α-helix | 186-202 | 17 | |
| α-helix | 216-225 | 10 | |
| α-helix | 227-235 | 9 | |
| α-helix | 243-256 | 14 | |
| α-helix | 283-285 | 3 | |
| β-strand | 287-292 | 6 | 7 |
| β-strand | 297-302 | 6 | 7 |
| α-helix | 303-314 | 12 | |
| α-helix | 316-318 | 3 | |
| α-helix | 325-327 | 3 | |
| α-helix | 329-343 | 15 | |
| α-helix | 344-347 | 4 | |
| α-helix | 381-390 | 10 | |
| β-strand | 392-395 | 4 | 11 |
| α-helix | 397-400 | 4 | |
| α-helix | 404-415 | 12 | |
| β-strand | 423-425 | 3 | 11 |
| α-helix | 429-433 | 5 | |
| α-helix | 435-444 | 10 | |
| α-helix | 451-454 | 4 | |
| α-helix | 457-467 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin-like protein ARP9 | A | protein | 476 | Saccharomyces cerevisiae | Q05123 (AlphaFold model) |
| Actin-related protein 7 | B | protein | 485 | Saccharomyces cerevisiae | Q12406 (AlphaFold model) |
>3WEE_1 Actin-like protein ARP9 (chains A) MDYKDDDDKGAPFRQDSILIIYPRSQTTLVQFGLNEETFTVPELEIPTQIYRTTRQDGSY TYHSTNKDNKAELIKPIQNGEIIDISAFTQFLRLIFVSILSDRANKNQDAFEAELSNIPL LLITHHSWSQSDLEIITQYVFESLEINNLIQLPASLAATYSMISLQNCCIIDVGTHHTDI IPIVDYAQLDHLVSSIPMGGQSINDSLKKLLPQWDDDQIESLKKSPIFEVLSDDAKKLSS FDFGNENEDEDEGTLNVAEIITSGRDTREVLEERERGQKVKNVKNSDLEFNTFWDEKGNE IKVGKQRFQGCNNLIKNISNRVGLTLDNIDDINKAKAVWENIIIVGGTTSISGFKEALLG QLLKDHLIIEPEEEKSKREEEAKSVLPAATKKKSKFMTNSTAFVPTIEYVQCPTVIKLAK YPDYFPEWKKSGYSEIIFLGAQIVSKQIFTHPKDTFYITREKYNMKGPAALWDVQF
>3WEE_2 Actin-related protein 7 (chains B) MTLNRKCVVIHNGSHRTVAGFSNVELPQCIIPSSYIKRTDEGGEAEFIFGTYNMIDAAAE KRNGDEVYTLVDSQGLPYNWDALEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMAIL ERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVTPIIDGIVVKNAVV RSKFGGDFLDFQVHERLAPLIKEENDMENMADEQKRSTDVWYEASTWIQQFKSTMLQVSE KDLFELERYYKEQADIYAKQQEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFKPLNKTLT LDLKECYQFAEYLFKPQLISDKFSPEDGLGPLMAKSVKKAGASINSMKANTSTNPNGLGT SHINTNVGDNNSTASSSNISPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQYK LTTFANQVMMDRKIQGWLGALTMANLPSWSLGKWYSKEDYETLKRDRKQSQATNATNPHH HHHHH
Water and common crystallization additives (SO4) are not listed.
Structure of the full-length yeast Arp7-Arp9 heterodimer. Lobsiger, J., Hunziker, Y., Richmond, T.J. Acta Crystallogr D Biol Crystallogr (2014) 70:310-316. DOI 10.1107/S1399004713027417 · PubMed
Other PDB entries of the same protein (UniProt Q05123 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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