7L3L: TRAF5 and TRAF6 RING Hetero dimer
Structure of TRAF5 and TRAF6 RING Hetero dimer. Determined by X-ray diffraction at 2.8 Å resolution. Released 17 Feb 2021.
- Method
- X-ray diffraction
- Resolution
- 2.8 Å
- Organism
- Homo sapiens
- Chains
- 4
- Atoms
- 3,894
- Mol. weight
- 58.76 kDa
- Ligands
- ZN
- Released
- 17 Feb 2021
Explore 7L3L in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7L3L contains 31 α-helices and 41 β-strands across 4 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.
Chain A: 8 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 35 | 1 | 1 |
| α-helix | 41-43 | 3 | |
| β-strand | 44 | 1 | 2 |
| β-strand | 51 | 1 | 2 |
| β-strand | 56-57 | 2 | 3 |
| β-strand | 63-64 | 2 | 3 |
| α-helix | 66-74 | 9 | |
| β-strand | 80 | 1 | 4 |
| β-strand | 87 | 1 | 4 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-95 | 2 | 3 |
| α-helix | 97-104 | 8 | |
| β-strand | 107-109 | 3 | 1 |
| β-strand | 119-121 | 3 | 1 |
| α-helix | 122-124 | 3 | |
| α-helix | 125-129 | 5 | |
| β-strand | 136 | 1 | 5 |
| β-strand | 149 | 1 | 5 |
| α-helix | 150-153 | 4 | |
| α-helix | 156-160 | 5 | |
Chain B: 7 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 56 | 1 | 6 |
| β-strand | 60 | 1 | 7 |
| α-helix | 63-65 | 3 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69 | 1 | 6 |
| β-strand | 76 | 1 | 6 |
| β-strand | 80-82 | 3 | 8 |
| β-strand | 88-90 | 3 | 8 |
| α-helix | 91-100 | 10 | |
| β-strand | 104 | 1 | 9 |
| β-strand | 111 | 1 | 9 |
| α-helix | 114-116 | 3 | |
| β-strand | 118-119 | 2 | 8 |
| α-helix | 121-129 | 9 | |
| β-strand | 131-133 | 3 | 7 |
| β-strand | 142-144 | 3 | 7 |
| α-helix | 145-147 | 3 | |
| α-helix | 148-152 | 5 | |
Chain C: 9 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 38-40 | 3 | |
| α-helix | 41-43 | 3 | |
| β-strand | 44 | 1 | 10 |
| β-strand | 51 | 1 | 10 |
| α-helix | 52 | 1 | |
| β-strand | 56-57 | 2 | 11 |
| β-strand | 63-64 | 2 | 11 |
| α-helix | 66-75 | 10 | |
| β-strand | 80 | 1 | 12 |
| β-strand | 87 | 1 | 12 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-95 | 2 | 11 |
| α-helix | 97-104 | 8 | |
| β-strand | 107-109 | 3 | 13 |
| β-strand | 119-121 | 3 | 13 |
| α-helix | 122-124 | 3 | |
| α-helix | 125-129 | 5 | |
| β-strand | 136-137 | 2 | 14 |
| β-strand | 148-149 | 2 | 14 |
| α-helix | 154-158 | 5 | |
Chain D: 7 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 56 | 1 | 15 |
| α-helix | 63-65 | 3 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69 | 1 | 15 |
| β-strand | 76 | 1 | 15 |
| β-strand | 80-82 | 3 | 16 |
| β-strand | 88-90 | 3 | 16 |
| α-helix | 91-100 | 10 | |
| β-strand | 102 | 1 | 1 |
| α-helix | 114-116 | 3 | |
| β-strand | 118-119 | 2 | 16 |
| α-helix | 121-128 | 8 | |
| α-helix | 145-147 | 3 | |
| α-helix | 148-151 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| TNF receptor-associated factor 5 | A, C | protein | 142 | Homo sapiens | O00463 (AlphaFold model) |
| TNF receptor-associated factor 6 | B, D | protein | 107 | Homo sapiens | Q9Y4K3 (AlphaFold model) |
Sequence of entity 1 (A, C), FASTA
>7L3L_1 TNF receptor-associated factor 5 (chains A, C)
ISLDFEPSIEYQFVERLEERYKCAFCHSVLHNPHQTGCGHRFCQHCILSLRELNTVPICP
VDKEVIKSQEVFKDNCCKREVLNLYVYCSNAPGCNAKVILGRYQDHLQQCLFQPVQCSNE
KCREPVLRKDLKEHLSASCQFR
Sequence of entity 2 (B, D), FASTA
>7L3L_2 TNF receptor-associated factor 6 (chains B, D)
EIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEI
LLENQLFPDNFAKREILSLMVKCPNEGCLHKMELRHLEDHQAHCEFA
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 14 |
Primary citation
The structure and ubiquitin binding properties of TRAF RING heterodimers. Das, A., Middleton, A.J., Padala, P. et al. J Mol Biol (2021):166844-166844. DOI 10.1016/j.jmb.2021.166844 · PubMed
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