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Amyloid fibril (in vitro) from full-length hnRNPA1 protein

Analyse Amyloid fibril (in vitro) from full-length hnRNPA1 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7ZJ2
Type
protein
Length
540 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.32
Source
Homo sapiens
Molecule
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1
UniProt
P09651
Pockets
2 · best druggability 0.50

Structure

electron microscopy · resolution 3.32 · 1 distinct chain · 0% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LIsoform A1-A of Heterogeneous nuclear ribonucleoprotein A1protein450% helix, 18% strandP09651

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12050.500.7635empty
22110.470.7433empty

Interfaces

38 interfaces between chains.

  • C–E · 1803 Ų buried · 59 hydrogen bonds · protein-protein
  • I–K · 1801 Ų buried · 59 hydrogen bonds · protein-protein
  • E–G · 1799 Ų buried · 59 hydrogen bonds · protein-protein
  • B–D · 1799 Ų buried · 59 hydrogen bonds · protein-protein
  • A–C · 1797 Ų buried · 59 hydrogen bonds · protein-protein

Compared structures

  • P09651 · AlphaFold monomer V2.0 prediction for heterogeneous nuclear ribonucleoprotein A1 (P09651) · a predicted model of the same protein · chain A against A, TM-score 0.32

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