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Pseudo-atomic model of the AKAP18-PKA complex in a linear conformation derived from electron microscopy

Analyse Pseudo-atomic model of the AKAP18-PKA complex in a linear conformation derived… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3J4R
Type
protein
Length
1,644 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
A-kinase anchor protein 18; Camp-dependent protein kinase type II-alpha regulatory…
EC
2.7.11.11
UniProt
Q8K1M3, P05132
Pockets
20 · best druggability 0.72

Structure

electron microscopy · 3 distinct chains · 36% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AA-kinase anchor protein 18protein23039% helix, 24% strand—
B, CCamp-dependent protein kinase type II-alpha regulatory subunitprotein38233% helix, 25% strandQ8K1M3
D, ECamp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11)protein32537% helix, 13% strandP05132

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19480.720.7666empty
29430.710.7571empty
35700.690.7864empty
42800.610.8041empty
53390.600.7734empty

Interfaces

5 interfaces between chains.

  • B–D · 1746 Ų buried · 28 hydrogen bonds · protein-protein
  • C–E · 1734 Ų buried · 26 hydrogen bonds · protein-protein
  • B–C · 734 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 313 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 309 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 3J4R · Pseudo-atomic model of the AKAP18-PKA Complex in a linear conformation derived from… · the same entry in another collection · chain A against A, TM-score 1.00

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