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Structure of the five-fold capsomer of the DARC1 capsid

Analyse Structure of the five-fold capsomer of the DARC1 capsid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6TAR
Type
protein
Length
820 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Activity-regulated cytoskeleton associated protein 1
UniProt
Q7K1U0
Pockets
14 · best druggability 0.65

Structure

electron microscopy · 1 distinct chain · 58% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, EActivity-regulated cytoskeleton associated protein 1protein16458% helix, 1% strandQ7K1U0

Pockets

14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15820.650.7676empty
25390.640.7686empty
35180.620.7561empty
43070.600.7839empty
53140.580.7737empty

Interfaces

5 interfaces between chains.

  • A–B · 1095 Ų buried · 5 hydrogen bonds · protein-protein
  • A–E · 1025 Ų buried · 4 hydrogen bonds · protein-protein
  • D–E · 1025 Ų buried · 3 hydrogen bonds · protein-protein
  • C–D · 1009 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 939 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 6TAR · Structure of the five-fold capsomer of the dArc1 capsid · the same entry in another collection · chain E against E, TM-score 1.00
  • Q7K1U0 · AlphaFold monomer V2.0 prediction for activity-regulated cytoskeleton associated protein… · a predicted model of the same protein · chain A against A, TM-score 0.93

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