Research workbench

Structural plasticity of helical nanotubes based on coiled-coil assemblies

Analyse Structural plasticity of helical nanotubes based on coiled-coil assemblies in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3J89
Type: protein
Length: 551 residues
Chains: 19
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Synthetic peptide
Pockets: 10 · best druggability 0.37

Structure

electron microscopy · 1 distinct chain · 93% helix, 0% 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, Q, R, S	Synthetic peptide	protein	29	93% helix, 0% strand	—

Pockets

10 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	113	0.37	0.74	16	empty
2	122	0.36	0.73	27	empty
3	110	0.35	0.73	24	empty
4	66	0.30	0.74	10	empty
5	74	0.30	0.73	14	empty

Interfaces

63 interfaces between chains.

G–K · 744 Å² buried · 5 hydrogen bonds · protein-protein
O–S · 744 Å² buried · 5 hydrogen bonds · protein-protein
D–H · 743 Å² buried · 5 hydrogen bonds · protein-protein
B–F · 742 Å² buried · 5 hydrogen bonds · protein-protein
E–I · 742 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

3J89 · Structural Plasticity of Helical Nanotubes Based on Coiled-Coil Assemblies · the same entry in another collection · chain A against A, 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
Elsewhere: RCSB PDB 3J89 · PDBe 3J89

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