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Crystal structure of repeats 8 and 9 of human erythroid spectrin

Analyse Crystal structure of repeats 8 and 9 of human erythroid spectrin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1S35
Type
protein
Length
211 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Spectrin beta chain, erythrocyte
UniProt
P11277
Ligands
SO4
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 87% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASpectrin beta chain, erythrocyteprotein21187% helix, 0% strandP11277

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · 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
1760.360.7616empty

Compared structures

  • 1S35 · Crystal Structure of Repeats 8 and 9 of Human Erythroid Spectrin · the same entry in another collection · chain A against A, TM-score 1.00
  • P11277 · AlphaFold monomer V2.0 prediction for spectrin beta chain, erythrocytic (P11277) · a predicted model of the same protein · chain A against A, TM-score 0.83

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