Research workbench

Dimer-of-dimer amyloid fibril structure of glucagon

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

PDB: 6NZN
Type: protein
Length: 464 residues
Chains: 16
Method: solid-state nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucagon
UniProt: P01275
Pockets: 10 · best druggability 0.84

Structure

solid-state nmr · 1 distinct chain · 0% helix, 86% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	Glucagon	protein	29	0% helix, 86% strand	P01275

Pockets

10 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	357	0.84	0.93	67	empty
2	152	0.80	0.97	30	empty
3	466	0.80	0.87	72	empty
4	79	0.73	0.97	17	empty
5	85	0.73	0.96	35	empty

Interfaces

52 interfaces between chains.

C–K · 1401 Å² buried · 44 hydrogen bonds · protein-protein
G–O · 1398 Å² buried · 48 hydrogen bonds · protein-protein
A–I · 1394 Å² buried · 45 hydrogen bonds · protein-protein
E–M · 1348 Å² buried · 41 hydrogen bonds · protein-protein
H–N · 1339 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

6NZN · Dimer-of-dimer amyloid fibril structure of glucagon · the same entry in another collection · chain H against H, 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 P01275
Elsewhere: RCSB PDB 6NZN · PDBe 6NZN · UniProt P01275

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