Crystal Structure of Reovirus Attachment Protein Sigma1 Trimer. Determined by X-ray diffraction at 2.6 Å resolution. Released 21 Dec 2001.
Explore 1KKE in 3D Show helices and sheets RCSB PDB PDBe
1KKE contains 19 α-helices and 67 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 |
|---|---|---|---|
| β-strand | 253-254 | 2 | 1 |
| β-strand | 257 | 1 | 2 |
| β-strand | 261-264 | 4 | 1 |
| β-strand | 270-272 | 3 | 1 |
| β-strand | 274 | 1 | 3 |
| β-strand | 279-281 | 3 | 4 |
| β-strand | 287-289 | 3 | 4 |
| α-helix | 290-295 | 6 | |
| β-strand | 296 | 1 | 5 |
| β-strand | 300-303 | 4 | 6 |
| β-strand | 306-309 | 4 | 6 |
| α-helix | 311-314 | 4 | |
| β-strand | 316-328 | 13 | 7 |
| β-strand | 331-344 | 14 | 7 |
| β-strand | 347-352 | 6 | 7 |
| α-helix | 353-354 | 2 | |
| β-strand | 355-358 | 4 | 7 |
| β-strand | 363-369 | 7 | 7 |
| β-strand | 374 | 1 | 7 |
| α-helix | 375 | 1 | |
| α-helix | 380-383 | 4 | |
| β-strand | 385 | 1 | 8 |
| β-strand | 394-404 | 11 | 7 |
| β-strand | 410-422 | 13 | 7 |
| β-strand | 425-431 | 7 | 7 |
| β-strand | 440-443 | 4 | 7 |
| α-helix | 444-445 | 2 | |
| β-strand | 446-451 | 6 | 7 |
| β-strand | 452 | 1 | 8 |
| α-helix | 453 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 257 | 1 | 1 |
| β-strand | 261-263 | 3 | 9 |
| β-strand | 269-272 | 4 | 9 |
| β-strand | 274 | 1 | 4 |
| β-strand | 279-281 | 3 | 10 |
| β-strand | 287-289 | 3 | 10 |
| β-strand | 296 | 1 | 6 |
| β-strand | 300-303 | 4 | 11 |
| β-strand | 306-309 | 4 | 11 |
| α-helix | 311-314 | 4 | |
| β-strand | 316-328 | 13 | 12 |
| β-strand | 331-344 | 14 | 12 |
| β-strand | 347-352 | 6 | 12 |
| α-helix | 353-354 | 2 | |
| β-strand | 355-358 | 4 | 12 |
| β-strand | 363-369 | 7 | 12 |
| β-strand | 374 | 1 | 12 |
| α-helix | 375 | 1 | |
| α-helix | 380-383 | 4 | |
| β-strand | 385 | 1 | 13 |
| β-strand | 394-404 | 11 | 12 |
| β-strand | 410-422 | 13 | 12 |
| β-strand | 425-431 | 7 | 12 |
| β-strand | 440-443 | 4 | 12 |
| α-helix | 444-445 | 2 | |
| β-strand | 446-451 | 6 | 12 |
| β-strand | 452 | 1 | 13 |
| α-helix | 453 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 256-257 | 2 | 9 |
| β-strand | 261-263 | 3 | 2 |
| β-strand | 270-272 | 3 | 2 |
| β-strand | 274 | 1 | 10 |
| β-strand | 279-281 | 3 | 3 |
| β-strand | 287-289 | 3 | 3 |
| β-strand | 296 | 1 | 11 |
| β-strand | 300-303 | 4 | 5 |
| β-strand | 306-309 | 4 | 5 |
| α-helix | 311-314 | 4 | |
| β-strand | 316-328 | 13 | 14 |
| β-strand | 331-344 | 14 | 14 |
| β-strand | 347-352 | 6 | 14 |
| α-helix | 353-354 | 2 | |
| β-strand | 355-358 | 4 | 14 |
| β-strand | 363-369 | 7 | 14 |
| β-strand | 374 | 1 | 14 |
| α-helix | 375 | 1 | |
| α-helix | 380-383 | 4 | |
| β-strand | 385 | 1 | 15 |
| β-strand | 394-404 | 11 | 14 |
| β-strand | 410-422 | 13 | 14 |
| β-strand | 425-431 | 7 | 14 |
| β-strand | 440-443 | 4 | 14 |
| α-helix | 444-445 | 2 | |
| β-strand | 446-451 | 6 | 14 |
| β-strand | 452 | 1 | 15 |
| α-helix | 453 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sigma 1 protein | A, B, C | protein | 210 | Mammalian orthoreovirus 3 | P03528 |
>1KKE_1 SIGMA 1 PROTEIN (chains A, B, C) IGATEQSYVASAVTPLRLNSSTKVLDMLIDSSTLEINSSGQLTVRSTSPNLRYPIADVSG GIGMSPNYRFRQSMWIGIVSYSGSGLNWRVQVNSDIFIVDDYIHICLPAFDGFSIADGGD LSLNFVTGLLPPLLTGDTEPAFHNDVVTYGAQTVAIGLSSGGAPQYMSKNLWVEQWQDGV LRLRVEGGGSITHSNSKWPAMTVSYPRSFT
Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber. Chappell, J.D., Prota, A.E., Dermody, T.S. et al. EMBO J (2002) 21:1-11. DOI 10.1093/emboj/21.1.1 · PubMed
Other PDB entries of the same protein (UniProt P03528), best resolution first:
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