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Cryo-EM structure of amyloid fibril formed by HNRNPA1 low complexity domain

Analyse Cryo-EM structure of amyloid fibril formed by HNRNPA1 low complexity domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BX7
Type: protein
Length: 270 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heterogeneous nuclear ribonucleoprotein A1
UniProt: P09651

Structure

electron microscopy · 1 distinct chain · 0% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Heterogeneous nuclear ribonucleoprotein A1	protein	45	0% helix, 42% strand	P09651

Interfaces

14 interfaces between chains.

A–B · 1772 Å² buried · 65 hydrogen bonds · protein-protein
E–F · 1765 Å² buried · 62 hydrogen bonds · protein-protein
B–C · 1760 Å² buried · 60 hydrogen bonds · protein-protein
D–E · 1739 Å² buried · 59 hydrogen bonds · protein-protein
A–D · 583 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

7BX7 · Cryo-EM structure of amyloid fibril formed by hnRNPA1 low complexity domain · the same entry in another collection · chain C against C, TM-score 1.00
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 0.27

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P09651
Elsewhere: RCSB PDB 7BX7 · PDBe 7BX7 · UniProt P09651

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