Structure of tnf receptor associated factor 2 (TRAF2). Determined by X-ray diffraction at 2.2 Å resolution. Released 12 Apr 1999.
Explore 1CA4 in 3D Show helices and sheets RCSB PDB PDBe
1CA4 contains 47 α-helices and 63 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 |
|---|---|---|---|
| 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 |
| α-helix | 464-466 | 3 | |
| β-strand | 467-474 | 8 | 2 |
| 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 |
| β-strand | 489-496 | 8 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 335-347 | 13 | |
| β-strand | 353-359 | 7 | 7 |
| α-helix | 361-369 | 9 | |
| β-strand | 375-377 | 3 | 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 |
| α-helix | 464-466 | 3 | |
| β-strand | 467-474 | 8 | 8 |
| 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 | 419-421 | 3 | |
| β-strand | 430-434 | 5 | 9 |
| β-strand | 443-447 | 5 | 9 |
| α-helix | 458-459 | 2 | |
| β-strand | 463 | 1 | 10 |
| α-helix | 464-466 | 3 | |
| β-strand | 467-474 | 8 | 10 |
| β-strand | 489-496 | 8 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (tnf receptor associated factor 2) | A, B, C, D, E, F | protein | 168 | Homo sapiens | Q12933 (AlphaFold model) |
>1CA4_1 PROTEIN (TNF RECEPTOR ASSOCIATED FACTOR 2) (chains A, B, C, D, E, F) AMADLEQKVLEMEASTYDGVFIWKISDFARKRQEAVAGRIPAIFSPAFYTSRYGYKMCLR IYLNGDGTGRGTHLSLFFVVMKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTS SSFQRPVNDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL
Structural basis for self-association and receptor recognition of human TRAF2. Park, Y.C., Burkitt, V., Villa, A.R. et al. Nature (1999) 398:533-538. DOI 10.1038/19110 · 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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