Research workbench
Structure of TNF receptor associated factor 2 (TRAF2)
Analyse Structure of TNF receptor associated factor 2 (TRAF2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CA4
- Type
- protein
- Length
- 1,008 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (TNF receptor associated factor 2)
- UniProt
- Q12933
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Protein (TNF receptor associated factor 2) | protein | 168 | 18% helix, 33% strand | Q12933 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1043 | 0.74 | 0.77 | 83 | empty |
| 2 | 1095 | 0.74 | 0.77 | 89 | empty |
| 3 | 111 | 0.37 | 0.74 | 24 | empty |
| 4 | 112 | 0.36 | 0.73 | 23 | empty |
| 5 | 119 | 0.36 | 0.73 | 22 | empty |
Interfaces
6 interfaces between chains.
- D–E · 580 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 568 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 567 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 565 Ų buried · 5 hydrogen bonds · protein-protein
- D–F · 561 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q12933
- Elsewhere: RCSB PDB 1CA4 · PDBe 1CA4 · UniProt Q12933
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.