MolNFT v1 · #95846 · protein
Crystal structure of axh domain complexed with capicua
4J2L · Ataxin-1: “Crystal structure of axh domain complexed with capicua”. X-ray diffraction, 1 pocket (best druggability 0.25). MolNFT v1 #95846 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4J2L
- Type
- protein
- Length
- 294 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ataxin-1; Protein capicua homolog
- UniProt
- P54253, Q96RK0
- Pockets
- 1 · best druggability 0.25
Structure
x-ray diffraction · 3 distinct chains · 20% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ataxin-1 | protein | 121 | 21% helix, 38% strand | P54253 |
| B | Ataxin-1 | protein | 123 | 19% helix, 41% strand | P54253 |
| C, D | Protein capicua homolog | protein | 25 | 16% helix, 36% strand | Q96RK0 |
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 | 51 | 0.25 | 0.72 | 12 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1016 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 911 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 837 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 385 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 335 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4J2L · Crystal Structure of AXH domain complexed with Capicua · the same entry in another collection · chain D against D, TM-score 1.00
- P54253 · AlphaFold monomer V2.0 prediction for ataxin-1 (P54253) · a predicted model of the same protein · chain B against A, TM-score 0.94
- Q96RK0 · AlphaFold monomer V2.0 prediction for protein capicua homolog (Q96RK0) · a predicted model of the same protein · chain C against A, TM-score 0.26
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 P54253
- Every structure of UniProt Q96RK0
- Elsewhere: RCSB PDB 4J2L · PDBe 4J2L · UniProt P54253 · UniProt Q96RK0
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