Research workbench

Amyloid fibril from the antimicrobial peptide aurein 3.3

Analyse Amyloid fibril from the antimicrobial peptide aurein 3.3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QV6
Type: protein
Length: 306 residues
Chains: 18
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aurein-3.3
UniProt: P82396
Pockets: 5 · best druggability 0.56

Structure

electron microscopy · 1 distinct chain · 0% helix, 76% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A, E, D, C, F, H, G, K, J, I, L, N, M, Q, P, O, R	Aurein-3.3	protein	17	0% helix, 76% strand	P82396

Pockets

5 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	294	0.56	0.76	32	empty
2	190	0.55	0.79	27	empty
3	224	0.52	0.76	20	empty
4	94	0.37	0.75	18	empty
5	50	0.27	0.74	10	empty

Interfaces

53 interfaces between chains.

C–I · 737 Å² buried · 18 hydrogen bonds · protein-protein
I–O · 735 Å² buried · 18 hydrogen bonds · protein-protein
A–G · 718 Å² buried · 16 hydrogen bonds · protein-protein
G–M · 717 Å² buried · 16 hydrogen bonds · protein-protein
D–J · 714 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

7QV6 · Amyloid fibril from the antimicrobial peptide aurein 3.3 · 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 P82396
Elsewhere: RCSB PDB 7QV6 · PDBe 7QV6 · UniProt P82396

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.