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Sheep connexin-50 at 1.9 ångströms resolution by cryoem

Analyse Sheep connexin-50 at 1.9 ångströms resolution by cryoem in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7JJP
Type
protein
Length
2,352 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 0.62

Structure

electron microscopy · 1 distinct chain · 70% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LGap junction alpha-8 proteinprotein19670% helix, 5% strandP55917

Ligands and binding sites

  • MC3 · 1,2-dimyristoyl-rac-glycero-3-phosphocholine · ligand · 180 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, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13620.620.7731empty
23680.610.7737empty
33400.610.7733empty
42810.600.7826empty
53210.600.7730empty

Interfaces

24 interfaces between chains.

  • H–I · 1398 Ų buried · 20 hydrogen bonds · protein-protein
  • E–F · 1396 Ų buried · 20 hydrogen bonds · protein-protein
  • A–F · 1395 Ų buried · 20 hydrogen bonds · protein-protein
  • I–J · 1394 Ų buried · 20 hydrogen bonds · protein-protein
  • C–D · 1394 Ų buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 36 disulfide (disulfide).

Compared structures

  • 7JJP · Sheep Connexin-50 at 1.9 angstroms resolution by CryoEM · the same entry in another collection · chain L against L, TM-score 1.00

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