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Human connexin 26 dodecamer at 90MMHG PCO2, PH7.4

Analyse Human connexin 26 dodecamer 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
7QEQ
Type
protein
Length
2,268 residues
Chains
12
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 0.79

Structure

electron microscopy · 1 distinct chain · 71% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LGap junction beta-2 proteinprotein18971% helix, 5% strandP29033

Ligands and binding sites

  • PTY · Phosphatidylethanolamine · ligand · 12 copies · chains A, F, B, C, D, E, G, L, H, I, J, K
  • LMT · Dodecyl-beta-D-maltoside · additive · 48 copies · chains A, B, C, D, E, F, 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, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17210.790.8367empty
28580.780.8173empty
36860.780.8265empty
48870.780.8077empty
58560.770.8075empty

Interfaces

24 interfaces between chains.

  • B–C · 1517 Ų buried · 23 hydrogen bonds · protein-protein
  • I–J · 1499 Ų buried · 22 hydrogen bonds · protein-protein
  • A–F · 1497 Ų buried · 20 hydrogen bonds · protein-protein
  • G–L · 1497 Ų buried · 23 hydrogen bonds · protein-protein
  • H–I · 1494 Ų buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 36 disulfide (disulfide).

Compared structures

  • 7QEQ · human Connexin 26 dodecamer at 90mmHg PCO2, pH7.4 · the same entry in another collection · chain L against L, TM-score 1.00

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