MolNFT v1 · #157024 · protein

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

6MM5 · Camp-dependent protein kinase catalytic subunit alpha: “Catalytic subunit of camp-dependent protein kinase a in complex with RYR2 peptide (2799-2810)”. X-ray diffraction, 2 ligands (ANP, MG), 6 pockets (best druggability 0.78).…

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).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Camp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11)	protein	338	37% helix, 16% strand	P05132
C	Ryanodine receptor 2	protein	12	0% helix, 17% strand	E9Q401

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	343	0.78	0.88	42	MG, ANP
2	101	0.46	0.80	16	empty
3	70	0.45	0.81	13	empty
4	79	0.34	0.75	16	empty
5	80	0.32	0.74	20	empty

Interfaces

1 interface between chains.

E–C · 744 Å² 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

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P05132
Every structure of UniProt E9Q401
Elsewhere: RCSB PDB 6MM5 · PDBe 6MM5 · UniProt P05132 · UniProt E9Q401

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