MolNFT v1 · #88649 · protein
The crystal structure of human muscle alpha-actinin-2
4D1E: “The crystal structure of human muscle alpha-actinin-2”. X-ray diffraction, 5 pockets (best druggability 0.79). MolNFT v1 #88649 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4D1E
- Type
- protein
- Length
- 859 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-actinin-2
- UniProt
- P35609
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-actinin-2 | protein | 859 | 70% helix, 1% strand | P35609 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 885 | 0.79 | 0.81 | 69 | empty |
| 2 | 94 | 0.38 | 0.76 | 19 | empty |
| 3 | 91 | 0.37 | 0.76 | 17 | empty |
| 4 | 50 | 0.35 | 0.79 | 9 | empty |
| 5 | 50 | 0.34 | 0.78 | 12 | empty |
Modifications
Observed in the structure: 13 modified (methylation).
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 P35609
- Elsewhere: RCSB PDB 4D1E · PDBe 4D1E · UniProt P35609
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