8IHU

Cryo-EM structure of an amyloid fibril formed by ALS-causing SOD1 mutation G85R


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.97 Å
  • Aggregation State: HELICAL ARRAY 
  • Reconstruction Method: HELICAL 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutations.

Wang, L.Q.Ma, Y.Y.Zhang, M.Y.Yuan, H.Y.Li, X.N.Zhao, K.Chen, J.Li, D.Wang, Z.Z.Le, W.D.Liu, C.Liang, Y.

(2024) Sci Adv 


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Superoxide dismutase [Cu-Zn]
A, B, C
154Homo sapiensMutation(s): 1 
Gene Names: SOD1
EC: 1.15.1.1
UniProt & NIH Common Fund Data Resources
Find proteins for P00441 (Homo sapiens)
Explore P00441 
Go to UniProtKB:  P00441
PHAROS:  P00441
GTEx:  ENSG00000142168 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00441
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.97 Å
  • Aggregation State: HELICAL ARRAY 
  • Reconstruction Method: HELICAL 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Natural Science Foundation of China (NSFC)China32271326
National Natural Science Foundation of China (NSFC)China32071212
National Natural Science Foundation of China (NSFC)China31770833
National Natural Science Foundation of China (NSFC)China32201040

Revision History  (Full details and data files)

  • Version 1.0: 2024-10-30
    Type: Initial release