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Crystal structure of camp-dependent protein kinase a (cho PKA) in complex with benzamide

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

PDB: 6SNX
Type: protein
Length: 340 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Camp-dependent protein kinase catalytic subunit alpha
EC: 2.7.11.11
UniProt: P25321
Ligands: UNU
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Camp-dependent protein kinase catalytic subunit alpha (EC 2.7.11.11)	protein	340	38% helix, 15% strand	P25321

Ligands and binding sites

UNU · Benzamide · ligand · 2 copies · chains A

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

Pockets

3 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	303	0.67	0.82	35	UNU
2	132	0.49	0.78	17	empty
3	61	0.30	0.75	18	empty

Modifications

Observed in the structure: 3 modified (phosphorylation).

Compared structures

6SNX · Crystal structure of cAMP-dependent protein kinase A (CHO PKA) in complex with benzamide · the same entry in another collection · chain A against A, 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 P25321
Elsewhere: RCSB PDB 6SNX · PDBe 6SNX · UniProt P25321

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