Co-crystal structure of SV40 large T antigen helicase domain and ADP. Determined by X-ray diffraction at 1.95 Å resolution. Released 19 Oct 2004.
Explore 1SVL in 3D Show helices and sheets RCSB PDB PDBe
1SVL contains 72 α-helices and 21 β-strands across 3 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 | 270-280 | 11 | |
| α-helix | 285-293 | 9 | |
| α-helix | 303-306 | 4 | |
| α-helix | 311-314 | 4 | |
| α-helix | 317-327 | 11 | |
| α-helix | 333-354 | 22 | |
| α-helix | 357-375 | 19 | |
| α-helix | 384-394 | 11 | |
| α-helix | 401-414 | 14 | |
| β-strand | 421-425 | 5 | 1 |
| α-helix | 432-443 | 12 | |
| β-strand | 446-448 | 3 | 1 |
| α-helix | 454-461 | 8 | |
| α-helix | 462-464 | 3 | |
| β-strand | 470-472 | 3 | 1 |
| α-helix | 481-483 | 3 | |
| α-helix | 485-487 | 3 | |
| α-helix | 490-494 | 5 | |
| α-helix | 498-502 | 5 | |
| β-strand | 507-509 | 3 | 2 |
| β-strand | 517-519 | 3 | 2 |
| α-helix | 520-522 | 3 | |
| β-strand | 524-528 | 5 | 1 |
| α-helix | 531-534 | 4 | |
| α-helix | 535-538 | 4 | |
| β-strand | 543-546 | 4 | 1 |
| α-helix | 551-558 | 8 | |
| α-helix | 562-565 | 4 | |
| α-helix | 572-582 | 11 | |
| α-helix | 585-587 | 3 | |
| α-helix | 593-606 | 14 | |
| α-helix | 609-621 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 270-280 | 11 | |
| α-helix | 285-293 | 9 | |
| α-helix | 294-296 | 3 | |
| α-helix | 303-306 | 4 | |
| α-helix | 311-314 | 4 | |
| α-helix | 317-327 | 11 | |
| α-helix | 333-354 | 22 | |
| α-helix | 357-375 | 19 | |
| α-helix | 384-394 | 11 | |
| α-helix | 401-414 | 14 | |
| β-strand | 421-425 | 5 | 3 |
| α-helix | 432-443 | 12 | |
| β-strand | 446-448 | 3 | 3 |
| α-helix | 457-461 | 5 | |
| α-helix | 462-464 | 3 | |
| β-strand | 470-472 | 3 | 3 |
| α-helix | 498-502 | 5 | |
| β-strand | 507-510 | 4 | 4 |
| α-helix | 512-514 | 3 | |
| β-strand | 516-519 | 4 | 4 |
| α-helix | 520-522 | 3 | |
| β-strand | 524-528 | 5 | 3 |
| α-helix | 535-538 | 4 | |
| β-strand | 541-546 | 6 | 3 |
| α-helix | 551-558 | 8 | |
| α-helix | 562-565 | 4 | |
| α-helix | 572-582 | 11 | |
| α-helix | 585-587 | 3 | |
| α-helix | 590-606 | 17 | |
| α-helix | 609-621 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 270-279 | 10 | |
| α-helix | 285-293 | 9 | |
| α-helix | 294-296 | 3 | |
| α-helix | 303-306 | 4 | |
| α-helix | 311-314 | 4 | |
| α-helix | 317-327 | 11 | |
| α-helix | 333-354 | 22 | |
| α-helix | 357-375 | 19 | |
| α-helix | 384-395 | 12 | |
| α-helix | 401-414 | 14 | |
| β-strand | 421-425 | 5 | 5 |
| α-helix | 432-443 | 12 | |
| β-strand | 446-448 | 3 | 5 |
| α-helix | 457-461 | 5 | |
| α-helix | 462-464 | 3 | |
| β-strand | 470-472 | 3 | 5 |
| α-helix | 480-483 | 4 | |
| α-helix | 490-495 | 6 | |
| α-helix | 498-502 | 5 | |
| β-strand | 507-509 | 3 | 6 |
| β-strand | 517-519 | 3 | 6 |
| α-helix | 520-522 | 3 | |
| β-strand | 524-528 | 5 | 5 |
| α-helix | 535-538 | 4 | |
| β-strand | 543-546 | 4 | 5 |
| α-helix | 551-558 | 8 | |
| α-helix | 562-565 | 4 | |
| α-helix | 572-582 | 11 | |
| α-helix | 585-587 | 3 | |
| α-helix | 590-606 | 17 | |
| α-helix | 609-620 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| large T antigen | A, B, C | protein | 377 | Simian virus 40 | P03070 (AlphaFold model) |
>1SVL_1 large T antigen (chains A, B, C) GLKEHDFNPEEAEETKQVSWKLVTEYAMETKCDDVLLLLGMYLEFQYSFEMCLKCIKKEQ PSHYKYHEKHYANAAIFADSKNQKTICQQAVDTVLAKKRVDSLQLTREQMLTNRFNDLLD RMDIMFGSTGSADIEEWMAGVAWLHCLLPKMDSVVYDFLKCMVYNIPKKRYWLFKGPIDS GKTTLAAALLELCGGKALNVNLPLDRLNFELGVAIDQFLVVFEDVKGTGGESRDLPSGQG INNLDNLRDYLDGSVKVNLEKKHLNKRTQIFPPGIVTMNEYSVPKTLQARFVKQIDFRPK DYLKHCLERSEFLLEKRIIQSGIALLLMLIWYRPVAEFAQSIQSRIVEWKERLDKEFSLS VYQKMKFNVAMGIGVLD
Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen. Gai, D., Zhao, R., Li, D. et al. Cell (2004) 119:47-60. DOI 10.1016/j.cell.2004.09.017 · PubMed
Other PDB entries of the same protein (UniProt P03070 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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