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Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 ångström resolution
Analyse Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EYN
- Type
- protein
- Length
- 229 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-actinin 1
- UniProt
- P12814
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-actinin 1 | protein | 229 | 62% helix, 2% strand | P12814 |
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 | 57 | 0.44 | 0.83 | 17 | empty |
Compared structures
- 2EYN · Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom… · the same entry in another collection · chain A against A, TM-score 1.00
- P12814 · AlphaFold monomer V2.0 prediction for alpha-actinin-1 (P12814) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P12814
- Elsewhere: RCSB PDB 2EYN · PDBe 2EYN · UniProt P12814
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