Research workbench
Solution structure of the death domain of nuclear matrix protein P84
Analyse Solution structure of the death domain of nuclear matrix protein P84 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WXP
- Type
- protein
- Length
- 110 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tho complex subunit 1
- UniProt
- Q96FV9
- Pockets
- 1 · best druggability 0.34
Structure
solution nmr · 1 distinct chain · 56% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tho complex subunit 1 | protein | 110 | 56% helix, 0% strand | Q96FV9 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.34 | 0.73 | 16 | empty |
Compared structures
- 1WXP · Solution structure of the death domain of nuclear matrix protein p84 · the same entry in another collection · chain A against A, TM-score 1.00
- Q96FV9 · AlphaFold monomer V2.0 prediction for tho complex subunit 1 (Q96FV9) · a predicted model of the same protein · chain A against A, TM-score 0.76
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 Q96FV9
- Elsewhere: RCSB PDB 1WXP · PDBe 1WXP · UniProt Q96FV9
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