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Cryo-EM structure of human PRP23-144 amyloid fibrils

Analyse Cryo-EM structure of human PRP23-144 amyloid fibrils in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7RL4
Type: protein
Length: 680 residues
Chains: 20
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major prion protein
UniProt: P04156
Pockets: 4 · best druggability 0.55

Structure

electron microscopy · 1 distinct chain · 0% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, K, P, C, G, L, Q, D, H, M, R, E, I, N, S, F, J, O, T	Major prion protein	protein	34	0% helix, 32% strand	P04156

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	349	0.55	0.74	36	empty
2	333	0.55	0.74	35	empty
3	293	0.54	0.75	32	empty
4	259	0.50	0.74	32	empty

Interfaces

61 interfaces between chains.

I–J · 1280 Å² buried · 31 hydrogen bonds · protein-protein
B–I · 1280 Å² buried · 31 hydrogen bonds · protein-protein
Q–R · 1279 Å² buried · 31 hydrogen bonds · protein-protein
B–H · 1278 Å² buried · 31 hydrogen bonds · protein-protein
P–S · 1278 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

7RL4 · Cryo-EM structure of human PrP23-144 amyloid fibrils · the same entry in another collection · chain K against K, TM-score 1.00

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 P04156
Elsewhere: RCSB PDB 7RL4 · PDBe 7RL4 · UniProt P04156

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