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Crystal structure of the actin-binding domain of human alpha-actinin-4

Analyse Crystal structure of the actin-binding domain of human alpha-actinin-4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6OA6
Type
protein
Length
227 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-actinin-4
UniProt
O43707
Pockets
1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 62% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-actinin-4protein22762% helix, 2% strandO43707

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1720.350.7617empty

Compared structures

  • 6OA6 · Crystal structure of the actin-binding domain of human alpha-actinin-4 · the same entry in another collection · chain A against A, TM-score 1.00
  • O43707 · AlphaFold monomer V2.0 prediction for alpha-actinin-4 (O43707) · a predicted model of the same protein · chain A against A, TM-score 0.98

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