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Cryo-EM structure of the consensus triskelion hub of the clathrin coat complex

Analyse Cryo-EM structure of the consensus triskelion hub of the clathrin coat complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SCT
Type
protein
Length
4,947 residues
Chains
15
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Clathrin heavy chain; Clathrin light chain
UniProt
C0MHR2, F1S398
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 5 distinct chains · 68% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, F, KClathrin heavy chainprotein37971% helix, 0% strandC0MHR2
B, G, LClathrin heavy chainprotein66666% helix, 0% strandC0MHR2
C, H, MClathrin heavy chainprotein44163% helix, 0% strandC0MHR2
D, I, NClathrin light chainprotein10472% helix, 0% strandF1S398
E, J, OClathrin light chainprotein5990% helix, 0% strandF1S398

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15590.820.8755empty
27360.780.8277empty
37240.770.8288empty
49820.770.7975empty
510030.760.7994empty

Interfaces

33 interfaces between chains.

  • A–D · 2180 Ų buried · 11 hydrogen bonds · protein-protein
  • F–I · 2175 Ų buried · 10 hydrogen bonds · protein-protein
  • K–N · 2168 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 1636 Ų buried · 14 hydrogen bonds · protein-protein
  • G–H · 1605 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 6SCT · Cryo-EM structure of the consensus triskelion hub of the clathrin coat complex · the same entry in another collection · chain A against A, TM-score 1.00

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