Crystal Structure of Reovirus T3D Attachment Protein Sigma1 head domain wild-type at 1.75 A resolution. Determined by X-ray diffraction at 1.75 Å resolution. Released 13 Feb 2007.
Explore 2OJ5 in 3D Show helices and sheets RCSB PDB PDBe
2OJ5 contains 39 α-helices and 96 β-strands across 6 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 | 296 | 1 | 1 |
| β-strand | 300-303 | 4 | 2 |
| β-strand | 306-309 | 4 | 2 |
| α-helix | 311-314 | 4 | |
| β-strand | 316-328 | 13 | 3 |
| β-strand | 331-344 | 14 | 3 |
| β-strand | 347-352 | 6 | 3 |
| α-helix | 353-354 | 2 | |
| β-strand | 355-358 | 4 | 3 |
| β-strand | 363-369 | 7 | 3 |
| β-strand | 374 | 1 | 3 |
| α-helix | 375 | 1 | |
| α-helix | 380-383 | 4 | |
| β-strand | 385 | 1 | 4 |
| β-strand | 394-404 | 11 | 3 |
| α-helix | 409 | 1 | |
| β-strand | 410-422 | 13 | 3 |
| β-strand | 425-431 | 7 | 3 |
| β-strand | 440-443 | 4 | 3 |
| α-helix | 444-445 | 2 | |
| β-strand | 446-451 | 6 | 3 |
| β-strand | 452 | 1 | 4 |
| α-helix | 453 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 296 | 1 | 2 |
| β-strand | 300-303 | 4 | 5 |
| β-strand | 306-309 | 4 | 5 |
| α-helix | 311-314 | 4 | |
| β-strand | 316-328 | 13 | 8 |
| β-strand | 331-344 | 14 | 8 |
| β-strand | 347-352 | 6 | 8 |
| α-helix | 353-354 | 2 | |
| β-strand | 355-357 | 3 | 8 |
| β-strand | 363-369 | 7 | 8 |
| β-strand | 374 | 1 | 8 |
| α-helix | 375 | 1 | |
| α-helix | 380-383 | 4 | |
| β-strand | 385 | 1 | 9 |
| β-strand | 394-404 | 11 | 8 |
| α-helix | 409 | 1 | |
| β-strand | 410-422 | 13 | 8 |
| β-strand | 425-431 | 7 | 8 |
| β-strand | 440-443 | 4 | 8 |
| α-helix | 444-445 | 2 | |
| β-strand | 446-451 | 6 | 8 |
| β-strand | 452 | 1 | 9 |
| α-helix | 453 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 296 | 1 | 10 |
| β-strand | 300-302 | 3 | 11 |
| β-strand | 307-309 | 3 | 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 |
| α-helix | 409 | 1 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 296 | 1 | 11 |
| β-strand | 300-303 | 4 | 14 |
| β-strand | 306-309 | 4 | 14 |
| α-helix | 311-314 | 4 | |
| β-strand | 316-328 | 13 | 17 |
| β-strand | 331-344 | 14 | 17 |
| β-strand | 347-352 | 6 | 17 |
| α-helix | 353-354 | 2 | |
| β-strand | 355-357 | 3 | 17 |
| β-strand | 363-369 | 7 | 17 |
| β-strand | 374 | 1 | 17 |
| α-helix | 375 | 1 | |
| α-helix | 380-383 | 4 | |
| β-strand | 385 | 1 | 18 |
| β-strand | 394-404 | 11 | 17 |
| β-strand | 410-422 | 13 | 17 |
| β-strand | 425-431 | 7 | 17 |
| β-strand | 440-443 | 4 | 17 |
| α-helix | 444-445 | 2 | |
| β-strand | 446-451 | 6 | 17 |
| β-strand | 452 | 1 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Viral attachment protein sigma 1 | A, B, C, D, E, F | protein | 165 | Reovirus sp. | P03528 |
>2OJ5_1 Viral attachment protein sigma 1 (chains A, B, C, D, E, F) GSSPNLRYPIADVSGGIGMSPNYRFRQSMWIGIVSYSGSGLNWRVQVNSDIFIVDDYIHI CLPAFDGFSIADGGDLSLNFVTGLLPPLLTGDTEPAFHNDVVTYGAQTVAIGLSSGGTPQ YMSKNLWVEQWQDGVLRLRVEGGGSITHSNSKWPAMTVSYPRSFT
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
Water and common crystallization additives (GOL) are not listed.
The Reovirus Sigma1 Aspartic Acid Sandwich: A TRIMERIZATION MOTIF POISED FOR CONFORMATIONAL CHANGE. Schelling, P., Guglielmi, K.M., Kirchner, E. et al. J Biol Chem (2007) 282:11582-11589. DOI 10.1074/jbc.M610805200 · PubMed
Other PDB entries of the same protein (UniProt P03528), best resolution first:
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