Research workbench
Oligomeric death domain complex
Analyse Oligomeric death domain complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OF5
- Type
- protein
- Length
- 1,137 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Death domain-containing protein cradd; Leucine-rich repeat and death domain-containing…
- UniProt
- P78560, Q9HB75
- Pockets
- 12 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Death domain-containing protein cradd | protein | 91 | 66% helix, 0% strand | P78560 |
| H, I, J, K, L | Leucine-rich repeat and death domain-containing protein | protein | 100 | 61% helix, 0% strand | Q9HB75 |
Pockets
12 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 983 | 0.85 | 0.86 | 105 | empty |
| 2 | 705 | 0.82 | 0.86 | 88 | empty |
| 3 | 235 | 0.81 | 0.94 | 39 | empty |
| 4 | 620 | 0.81 | 0.86 | 56 | empty |
| 5 | 291 | 0.79 | 0.91 | 37 | empty |
Interfaces
37 interfaces between chains.
- B–H · 577 Ų buried · 15 hydrogen bonds · protein-protein
- E–K · 547 Ų buried · 5 hydrogen bonds · protein-protein
- H–L · 537 Ų buried · 6 hydrogen bonds · protein-protein
- I–J · 530 Ų buried · 5 hydrogen bonds · protein-protein
- D–F · 529 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2OF5 · Oligomeric Death Domain complex · the same entry in another collection · chain L against L, TM-score 1.00
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 P78560
- Every structure of UniProt Q9HB75
- Elsewhere: RCSB PDB 2OF5 · PDBe 2OF5 · UniProt P78560 · UniProt Q9HB75
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