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Catalytic subunit of camp-dependent protein kinase a in complex with RYR2 peptide (2799-2810)

Analyse Catalytic subunit of camp-dependent protein kinase a in complex with RYR2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6MM5
Type
protein
Length
350 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Camp-dependent protein kinase catalytic subunit alpha; Ryanodine receptor 2
EC
2.7.11.11
UniProt
P05132, E9Q401
Ligands
ANP, MG
Pockets
6 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ECamp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11)protein33837% helix, 16% strandP05132
CRyanodine receptor 2protein120% helix, 17% strandE9Q401

Ligands and binding sites

  • ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains E, C
  • MG · Magnesium ion · metal · chains E
  • EDO · 1,2-ethanediol · additive · chains E, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13430.780.8842MG, ANP
21010.460.8016empty
3700.450.8113empty
4790.340.7516empty
5800.320.7420empty

Interfaces

1 interface between chains.

  • E–C · 744 Ų buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

  • 6MM5 · Catalytic subunit of cAMP-dependent protein kinase A in complex with RyR2 peptide… · the same entry in another collection · chain E against E, TM-score 1.00

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