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Sheep Connexin-50 at 2.5 angstroms reoslution, Lipid Class 2

Analyse Sheep Connexin-50 at 2.5 angstroms reoslution, Lipid Class 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7JM9
Type
protein
Length
2,328 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.5
Source
Ovis aries
Molecule
Gap junction alpha-8 protein
UniProt
P55917
Ligands
MC3
Pockets
20 · best druggability 0.64

Structure

electron microscopy · resolution 2.5 · 1 distinct chain · 71% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LGap junction alpha-8 proteinprotein19471% helix, 5% strandP55917

Ligands and binding sites

  • MC3 · 1,2-dimyristoyl-rac-glycero-3-phosphocholine · ligand · 168 copies · chains A, F, B, C, D, E, G, L, H, 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
14370.640.7743empty
24150.630.7741empty
34140.630.7743empty
43850.630.7734empty
54110.630.7743empty

Interfaces

24 interfaces between chains.

  • J–K · 1409 Ų buried · 12 hydrogen bonds · protein-protein
  • D–E · 1409 Ų buried · 12 hydrogen bonds · protein-protein
  • I–J · 1409 Ų buried · 12 hydrogen bonds · protein-protein
  • E–F · 1408 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 1407 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 36 disulfide (disulfide).

Compared structures

  • 7JM9 · Sheep connexin-50 at 2.5 ångströms reoslution, lipid class 2 · the same entry in another collection · chain L against L, TM-score 1.00

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