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Crystal structure of the rod domain of alpha-actinin

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

PDB
1HCI
Type
protein
Length
950 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-actinin 2
UniProt
P35609
Pockets
14 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAlpha-actinin 2protein47578% helix, 0% strandP35609

Pockets

14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14020.610.7648empty
22830.560.7634empty
32280.540.7729empty
41780.520.7825empty
51630.500.7824empty

Interfaces

1 interface between chains.

  • A–B · 3456 Ų buried · 21 hydrogen bonds · protein-protein

Compared structures

  • 1HCI · Crystal structure of the rod domain of alpha-actinin · the same entry in another collection · chain A against A, TM-score 1.00
  • P35609 · AlphaFold monomer V2.0 prediction for alpha-actinin-2 (P35609) · a predicted model of the same protein · chain B against A, TM-score 0.52

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