MolNFT v1 · #146861 · protein
Crystal structure of the alpha-N-catenin actin-binding domain H1 mutant
6DUY · Catenin alpha-2: “Crystal structure of the alpha-N-catenin actin-binding domain H1 mutant”. X-ray diffraction, 4 pockets (best druggability 0.50). MolNFT v1 #146861 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6DUY
- Type
- protein
- Length
- 381 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catenin alpha-2
- UniProt
- Q61301
- Pockets
- 4 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catenin alpha-2 | protein | 191 | 70% helix, 5% strand | Q61301 |
| B | Catenin alpha-2 | protein | 190 | 70% helix, 5% strand | Q61301 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 223 | 0.50 | 0.76 | 30 | empty |
| 2 | 97 | 0.37 | 0.75 | 16 | empty |
| 3 | 66 | 0.32 | 0.75 | 12 | empty |
| 4 | 78 | 0.31 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 587 Ų buried · 5 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 Q61301
- Elsewhere: RCSB PDB 6DUY · PDBe 6DUY · UniProt Q61301
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