Structure of tnf receptor associated factor 2 (TRAF2) in complex with a human OX40 peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 8 Mar 2000.
Explore 1D0A in 3D Show helices and sheets RCSB PDB PDBe
1D0A contains 52 α-helices and 72 β-strands across 12 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 | 335-347 | 13 | |
| β-strand | 353-359 | 7 | 1 |
| α-helix | 361-369 | 9 | |
| β-strand | 376-377 | 2 | 2 |
| α-helix | 378-380 | 3 | |
| β-strand | 381-382 | 2 | 2 |
| β-strand | 389-395 | 7 | 2 |
| α-helix | 400-402 | 3 | |
| β-strand | 406-414 | 9 | 2 |
| α-helix | 419-421 | 3 | |
| β-strand | 430-434 | 5 | 1 |
| β-strand | 443-447 | 5 | 1 |
| α-helix | 454-456 | 3 | |
| α-helix | 458-459 | 2 | |
| β-strand | 463 | 1 | 2 |
| β-strand | 467-474 | 8 | 2 |
| α-helix | 476-480 | 5 | |
| β-strand | 486 | 1 | 1 |
| β-strand | 489-496 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 335-347 | 13 | |
| β-strand | 353-359 | 7 | 3 |
| α-helix | 361-369 | 9 | |
| β-strand | 376-377 | 2 | 4 |
| α-helix | 378-380 | 3 | |
| β-strand | 381-382 | 2 | 4 |
| β-strand | 389-395 | 7 | 4 |
| α-helix | 400-402 | 3 | |
| β-strand | 406-414 | 9 | 4 |
| α-helix | 419-421 | 3 | |
| β-strand | 430-434 | 5 | 3 |
| β-strand | 443-447 | 5 | 3 |
| α-helix | 454-456 | 3 | |
| α-helix | 458-459 | 2 | |
| β-strand | 463 | 1 | 4 |
| α-helix | 464-466 | 3 | |
| β-strand | 467-474 | 8 | 4 |
| α-helix | 476-480 | 5 | |
| β-strand | 486 | 1 | 3 |
| β-strand | 489-496 | 8 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 337-347 | 11 | |
| β-strand | 353-359 | 7 | 7 |
| α-helix | 361-369 | 9 | |
| β-strand | 376-377 | 2 | 8 |
| α-helix | 378-380 | 3 | |
| β-strand | 381-382 | 2 | 8 |
| β-strand | 389-395 | 7 | 8 |
| α-helix | 400-402 | 3 | |
| β-strand | 406-414 | 9 | 8 |
| α-helix | 419-421 | 3 | |
| β-strand | 430-434 | 5 | 7 |
| β-strand | 443-447 | 5 | 7 |
| α-helix | 454-456 | 3 | |
| α-helix | 458-459 | 2 | |
| β-strand | 463 | 1 | 8 |
| β-strand | 467-474 | 8 | 8 |
| α-helix | 476-480 | 5 | |
| β-strand | 486 | 1 | 7 |
| β-strand | 489-496 | 8 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 335-347 | 13 | |
| β-strand | 353-359 | 7 | 9 |
| α-helix | 361-369 | 9 | |
| β-strand | 376-377 | 2 | 10 |
| α-helix | 378-380 | 3 | |
| β-strand | 381-382 | 2 | 10 |
| β-strand | 389-395 | 7 | 10 |
| α-helix | 400-402 | 3 | |
| β-strand | 406-414 | 9 | 10 |
| α-helix | 415-416 | 2 | |
| α-helix | 419-421 | 3 | |
| β-strand | 430-434 | 5 | 9 |
| β-strand | 443-447 | 5 | 9 |
| α-helix | 454-456 | 3 | |
| α-helix | 458-459 | 2 | |
| β-strand | 463 | 1 | 10 |
| α-helix | 464-466 | 3 | |
| β-strand | 467-474 | 8 | 10 |
| α-helix | 476-480 | 5 | |
| β-strand | 486 | 1 | 9 |
| β-strand | 489-496 | 8 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 263-264 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tumor necrosis factor receptor associated protein 2 | A, B, C, D, E, F | protein | 168 | Homo sapiens | Q12933 (AlphaFold model) |
| OX40L receptor peptide | G, H, I, J, K, L | protein | 6 | P43489 (AlphaFold model) |
>1D0A_1 TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 2 (chains A, B, C, D, E, F) AMADLEQKVLEMEASTYDGVFIWKISDFPRKRQEAVAGRIPAIFSPAFYTSRYGYKMCLR IYLNGDGTGRGTHLSLFFVVMKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTS SSFQRPVNDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL
>1D0A_2 OX40L RECEPTOR PEPTIDE (chains G, H, I, J, K, L) XPIQEE
The structural basis for the recognition of diverse receptor sequences by TRAF2. Ye, H., Park, Y.C., Kreishman, M. et al. Mol Cell (1999) 4:321-330. DOI 10.1016/S1097-2765(00)80334-2 · PubMed
Other PDB entries of the same protein (UniProt Q12933 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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