Research workbench
The structure of the A20-binding inhibitor of nf-kb 1 in complex with tri-ubiquitin
Analyse The structure of the A20-binding inhibitor of nf-kb 1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EAO
- Type
- protein
- Length
- 349 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyubiquitin-C; TNFAIP3-interacting protein 1
- UniProt
- P0CG48, Q15025
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 3 distinct chains · 47% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyubiquitin-C | protein | 224 | 21% helix, 34% strand | P0CG48 |
| B | TNFAIP3-interacting protein 1 | protein | 63 | 94% helix, 0% strand | Q15025 |
| C | TNFAIP3-interacting protein 1 | protein | 62 | 95% helix, 0% strand | Q15025 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 178 | 0.45 | 0.74 | 21 | empty |
| 2 | 59 | 0.30 | 0.74 | 11 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1815 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 841 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 495 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7EAO · The structure of the A20-binding inhibitor of NF-kB 1 in complex with tri-ubiquitin · the same entry in another collection · chain A against A, TM-score 1.00
- Q15025 · AlphaFold monomer V2.0 prediction for TNFAIP3-interacting protein 1 (Q15025) · a predicted model of the same protein · chain B against A, TM-score 0.88
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 P0CG48
- Every structure of UniProt Q15025
- Elsewhere: RCSB PDB 7EAO · PDBe 7EAO · UniProt P0CG48 · UniProt Q15025
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