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Clathrin heavy chain N-terminal domain complexed with peptide from protein mu-ns of reovirus type 1

Analyse Clathrin heavy chain N-terminal domain complexed with peptide from protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7BN1
Type
protein
Length
738 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Clathrin heavy chain 1; Protein mu-ns from reovirus type 1
UniProt
Q00610
Pockets
5 · best druggability 0.83

Structure

x-ray diffraction · 4 distinct chains · 9% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AClathrin heavy chain 1protein3619% helix, 51% strandQ00610
BClathrin heavy chain 1protein3609% helix, 51% strandQ00610
EProtein mu-ns from reovirus type 1protein80% helix, 13% strand—
FProtein mu-ns from reovirus type 1protein90% helix, 11% strand—

Ligands and binding sites

  • PG4 · Tetraethylene glycol · additive · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111380.830.84117empty
26870.750.8073empty
3720.330.7617empty
4610.320.7617empty
5530.250.7317empty

Interfaces

3 interfaces between chains.

  • A–B · 1035 Ų buried · 14 hydrogen bonds · protein-protein
  • B–F · 533 Ų buried · 4 hydrogen bonds · protein-protein
  • A–E · 509 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 7BN1 · Clathrin heavy chain N-terminal domain complexed with peptide from Protein mu-NS of… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q00610 · AlphaFold monomer V2.0 prediction for clathrin heavy chain 1 (Q00610) · a predicted model of the same protein · chain B against A, TM-score 0.99

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