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Crystal structure of di-phosphorylated human CLK1 in complex with 4- (1H-indol-3-YL)PYRIMIDIN-2-amine

Analyse Crystal structure of di-phosphorylated human CLK1 in complex with 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7O9Y
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dual specificity protein kinase CLK1
EC: 2.7.12.1
UniProt: P49759
Ligands: V5T
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dual specificity protein kinase CLK1 (EC 2.7.12.1)	protein	330	39% helix, 21% strand	P49759

Ligands and binding sites

V5T · 4-(1~{H}-indol-3-yl)pyrimidin-2-amine · ligand · chains A

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

Pockets

2 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	325	0.66	0.81	45	V5T
2	93	0.41	0.78	18	empty

Compared structures

7O9Y · Crystal structure of di-phosphorylated human CLK1 in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
P49759 · AlphaFold monomer V2.0 prediction for dual specificity protein kinase CLK1 (P49759) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P49759
Elsewhere: RCSB PDB 7O9Y · PDBe 7O9Y · UniProt P49759

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