Crystal Structure of TRAF2. Determined by X-ray diffraction at 2.67 Å resolution. Released 28 Apr 2010.
Explore 3M06 in 3D Show helices and sheets RCSB PDB PDBe
3M06 contains 9 α-helices and 0 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 | 268-326 | 59 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 268-306 | 39 | |
| α-helix | 313-316 | 4 | |
| α-helix | 318-324 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 268-327 | 60 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 268-324 | 57 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 268-295 | 28 | |
| α-helix | 299-325 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| TNF receptor-associated factor 2 | A, B, C, D, E, F | protein | 72 | Homo sapiens | Q12933 (AlphaFold model) |
>3M06_1 TNF receptor-associated factor 2 (chains A, B, C, D, E, F) SELLQRCESLEKKTATFENIVCVLNREVERVAMTAEACSRQHRLDQDKIEALSSKVQQLE RSIGLEHHHHHH
Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation. Zheng, C., Kabaleeswaran, V., Wang, Y. et al. Mol Cell (2010) 38:101-113. DOI 10.1016/j.molcel.2010.03.009 · 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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