Research workbench

Human connexin-26 (low pH open conformation)

Analyse Human connexin-26 (low pH open conformation) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UVS
Type: protein
Length: 1,920 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gap junction beta-2 protein
UniProt: P29033
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 64% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, K, L, B, H, C, I, D, J, E, F, G	Gap junction beta-2 protein	protein	160	64% helix, 6% strand	P29033

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1028	0.84	0.85	163	empty
2	727	0.79	0.83	93	empty
3	720	0.79	0.83	99	empty
4	700	0.78	0.83	96	empty
5	478	0.77	0.85	86	empty

Interfaces

24 interfaces between chains.

A–I · 369 Å² buried · 0 hydrogen bonds · protein-protein
H–D · 359 Å² buried · 0 hydrogen bonds · protein-protein
K–F · 358 Å² buried · 0 hydrogen bonds · protein-protein
L–E · 355 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 355 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6UVS · Human Connexin-26 (Low pH open conformation) · the same entry in another collection · chain G against G, 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 P29033
Elsewhere: RCSB PDB 6UVS · PDBe 6UVS · UniProt P29033

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