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Sheep connexin-50 at 2.5 ångströms resolution, lipid class 3

Analyse Sheep connexin-50 at 2.5 ångströms resolution, lipid class 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7JMC
Type
protein
Length
2,304 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gap junction alpha-8 protein
UniProt
P55917
Ligands
MC3
Pockets
20 · best druggability 0.64

Structure

electron microscopy · 1 distinct chain · 73% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LGap junction alpha-8 proteinprotein19273% helix, 5% strandP55917

Ligands and binding sites

  • MC3 · 1,2-dimyristoyl-rac-glycero-3-phosphocholine · ligand · 144 copies · chains A, B, F, C, D, E, G, H, L, I, J, K

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14480.640.7739empty
23870.630.7832empty
34000.630.7731empty
43950.630.7731empty
53970.620.7731empty

Interfaces

24 interfaces between chains.

  • C–D · 1393 Ų buried · 13 hydrogen bonds · protein-protein
  • K–L · 1391 Ų buried · 13 hydrogen bonds · protein-protein
  • I–J · 1391 Ų buried · 13 hydrogen bonds · protein-protein
  • E–F · 1391 Ų buried · 13 hydrogen bonds · protein-protein
  • G–H · 1389 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 36 disulfide (disulfide).

Compared structures

  • 7JMC · Sheep Connexin-50 at 2.5 angstroms resolution, Lipid Class 3 · the same entry in another collection · chain L against L, TM-score 1.00

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