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Binary complex of metal-free pkac with SP20.

Analyse Binary complex of metal-free pkac with SP20. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4O22
Type: protein
Length: 359 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Camp-dependent protein kinase catalytic subunit alpha.; Phosphorylated peptide PSP20.
EC: 2.7.11.11
UniProt: P05132, P61925
Pockets: 5 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Camp-dependent protein kinase catalytic subunit alpha. (EC 2.7.11.11)	protein	339	38% helix, 16% strand	P05132
S	Phosphorylated peptide PSP20.	protein	20	30% helix, 10% strand	P61925

Pockets

5 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	383	0.78	0.87	44	empty
2	74	0.43	0.80	15	empty
3	95	0.41	0.78	19	empty
4	87	0.35	0.75	16	empty
5	72	0.31	0.74	16	empty

Interfaces

1 interface between chains.

A–S · 1018 Å² buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (phosphorylation).

Compared structures

4O22 · Binary complex of metal-free PKAc with SP20. · the same entry in another collection · chain S against S, 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 P61925
Elsewhere: RCSB PDB 4O22 · PDBe 4O22 · UniProt P05132 · UniProt P61925

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