MolNFT v1 · #51048 · protein

Structure of PKA-pkb chimera complexed with 6-(4-(4-(4- chloro-phenyl)-piperidin-4-yl)-phenyl)-9H-purine

2UW0 · Camp-dependent protein kinase, alpha-catalytic subunit: “Structure of PKA-pkb chimera complexed with 6-(4-(4-(4- chloro-phenyl)-piperidin-4-yl)-phenyl)-9H-purine”. X-ray diffraction, 1 ligand (GVK), 5 pockets (best druggability…

PDB: 2UW0
Type: protein
Length: 357 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Camp-dependent protein kinase, alpha-catalytic subunit; Camp-dependent protein kinase…
UniProt: P00517, P61925
Ligands: GVK
Pockets: 5 · best druggability 0.79

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Camp-dependent protein kinase, alpha-catalytic subunit	protein	337	37% helix, 17% strand	P00517
I	Camp-dependent protein kinase inhibitor alpha	protein	20	30% helix, 10% strand	P61925

Ligands and binding sites

GVK · 6-{4-[4-(4-chlorophenyl)piperidin-4-yl]phenyl}-9H-purine · ligand · chains A, I

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

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	404	0.79	0.88	42	GVK
2	70	0.41	0.79	13	empty
3	102	0.40	0.77	23	empty
4	78	0.34	0.75	14	empty
5	62	0.27	0.73	14	empty

Interfaces

1 interface between chains.

A–I · 1072 Å² buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (phosphorylation).

Compared structures

2UW0 · Structure of PKA-PKB chimera complexed with 6-(4-(4-(4-Chloro-phenyl)… · the same entry in another collection · chain A against A, TM-score 1.00
P61925 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase inhibitor alpha… · a predicted model of the same protein · chain I against A, TM-score 0.41

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 P00517
Every structure of UniProt P61925
Elsewhere: RCSB PDB 2UW0 · PDBe 2UW0 · UniProt P00517 · UniProt P61925

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