MolNFT v1 · #120456 · protein
TRAF1-tank complex
5H10 · TNF receptor-associated factor 1: “TRAF1-tank complex”. X-ray diffraction, 6 pockets (best druggability 0.74). MolNFT v1 #120456 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5H10
- Type
- protein
- Length
- 598 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TNF receptor-associated factor 1; Traf family member-associated nf-kappab activator
- UniProt
- Q13077
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 6 distinct chains · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TNF receptor-associated factor 1 | protein | 192 | 31% helix, 28% strand | Q13077 |
| B | TNF receptor-associated factor 1 | protein | 190 | 33% helix, 28% strand | Q13077 |
| C | TNF receptor-associated factor 1 | protein | 195 | 32% helix, 29% strand | Q13077 |
| D | Traf family member-associated nf-kappab activator | protein | 6 | 0% helix, 33% strand | — |
| E | Traf family member-associated nf-kappab activator | protein | 7 | 0% helix, 29% strand | — |
| F | Traf family member-associated nf-kappab activator | protein | 8 | 0% helix, 25% strand | — |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 802 | 0.74 | 0.78 | 71 | empty |
| 2 | 341 | 0.62 | 0.78 | 42 | empty |
| 3 | 110 | 0.39 | 0.75 | 17 | empty |
| 4 | 80 | 0.31 | 0.73 | 13 | empty |
| 5 | 73 | 0.30 | 0.73 | 17 | empty |
Interfaces
6 interfaces between chains.
- A–C · 1251 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 1207 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1190 Ų buried · 9 hydrogen bonds · protein-protein
- C–F · 523 Ų buried · 10 hydrogen bonds · protein-protein
- B–E · 441 Ų buried · 8 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 Q13077
- Elsewhere: RCSB PDB 5H10 · PDBe 5H10 · UniProt Q13077
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