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Cryo-EM structure of human AA amyloid fibril

Analyse Cryo-EM structure of human AA amyloid fibril in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6MST
Type
protein
Length
648 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.7
Source
Homo sapiens
Molecule
Serum amyloid A-1 protein
UniProt
P0DJI8
Pockets
10 · best druggability 0.73

Structure

electron microscopy · resolution 2.7 · 1 distinct chain · 0% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, E, D, F, H, I, J, K, L, GSerum amyloid A-1 proteinprotein540% helix, 46% strandP0DJI8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11980.730.9034empty
22040.730.8936empty
31220.640.8827empty
41210.620.8729empty
5590.510.8623empty

Interfaces

45 interfaces between chains.

  • A–C · 2557 Ų buried · 76 hydrogen bonds · protein-protein
  • I–K · 2552 Ų buried · 73 hydrogen bonds · protein-protein
  • J–L · 2544 Ų buried · 72 hydrogen bonds · protein-protein
  • B–D · 2537 Ų buried · 72 hydrogen bonds · protein-protein
  • I–G · 2536 Ų buried · 73 hydrogen bonds · protein-protein

Compared structures

  • 6MST · Cryo-EM structure of human aa amyloid fibril · the same entry in another collection · chain L against L, TM-score 1.00

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