Research workbench

Human connexin 26 class 2 hexamer at 90MMHG PCO2, PH7.4

Analyse Human connexin 26 class 2 hexamer at 90MMHG PCO2, PH7.4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QEW
Type: protein
Length: 1,128 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gap junction beta-2 protein
UniProt: P29033
Ligands: PTY
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 66% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
G, H, I, J, K, L	Gap junction beta-2 protein	protein	188	66% helix, 5% strand	P29033

Ligands and binding sites

PTY · Phosphatidylethanolamine · ligand · 6 copies · chains G, L, H, I, J, K
LMT · Dodecyl-beta-D-maltoside · additive · 24 copies · chains G, H, I, J, K, L

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	331	0.81	0.91	52	empty
2	300	0.80	0.91	49	empty
3	287	0.80	0.91	55	empty
4	195	0.77	0.92	34	empty
5	193	0.76	0.91	34	empty

Interfaces

6 interfaces between chains.

H–I · 1436 Å² buried · 21 hydrogen bonds · protein-protein
K–L · 1423 Å² buried · 23 hydrogen bonds · protein-protein
I–J · 1415 Å² buried · 23 hydrogen bonds · protein-protein
G–H · 1385 Å² buried · 18 hydrogen bonds · protein-protein
G–L · 1382 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

7QEW · human Connexin 26 class 2 hexamer at 90mmHg PCO2, pH7.4 · the same entry in another collection · chain L against L, TM-score 1.00
P29033 · AlphaFold monomer V2.0 prediction for gap junction beta-2 protein (P29033) · a predicted model of the same protein · chain J against A, TM-score 0.95

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 7QEW · PDBe 7QEW · UniProt P29033

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