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Crystal structure of the traf domain of TRAF5
Analyse Crystal structure of the traf domain of TRAF5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GJH
- Type
- protein
- Length
- 528 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TNF receptor-associated factor 5
- UniProt
- P70191
- Pockets
- 8 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 22% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TNF receptor-associated factor 5 | protein | 175 | 22% helix, 32% strand | P70191 |
| B | TNF receptor-associated factor 5 | protein | 176 | 20% helix, 32% strand | P70191 |
| C | TNF receptor-associated factor 5 | protein | 177 | 23% helix, 32% strand | P70191 |
Pockets
8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 324 | 0.68 | 0.82 | 42 | empty |
| 2 | 262 | 0.61 | 0.80 | 28 | empty |
| 3 | 294 | 0.60 | 0.78 | 31 | empty |
| 4 | 184 | 0.56 | 0.80 | 27 | empty |
| 5 | 225 | 0.56 | 0.78 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–C · 786 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 779 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 752 Ų buried · 6 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 P70191
- Elsewhere: RCSB PDB 4GJH · PDBe 4GJH · UniProt P70191
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