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Human connexin-26 (neutral pH open conformation)

Analyse Human connexin-26 (neutral 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
6UVR
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 0.76

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, K, L, B, H, C, I, D, J, E, F, GGap junction beta-2 proteinprotein16064% helix, 6% strandP29033

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14360.760.8558empty
25440.760.8363empty
34240.760.8556empty
44480.760.8458empty
53670.750.8549empty

Interfaces

24 interfaces between chains.

  • H–D · 937 Ų buried · 5 hydrogen bonds · protein-protein
  • J–F · 930 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 921 Ų buried · 5 hydrogen bonds · protein-protein
  • J–E · 918 Ų buried · 6 hydrogen bonds · protein-protein
  • A–I · 917 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 36 disulfide (disulfide).

Compared structures

  • 6UVR · Human Connexin-26 (Neutral pH open conformation) · the same entry in another collection · chain G against G, TM-score 1.00

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