MolNFT v1 · #149373 · protein

X-ray structure of CLK2-KD(136-496)/CX-4945 at 1.95A

6FYL · Dual specificity protein kinase CLK2: “X-ray structure of CLK2-KD(136-496)/CX-4945 at 1.95A”. X-ray diffraction, 1 ligand (3NG), 2 pockets (best druggability 0.63). MolNFT v1 #149373 on GenesisL1: 3D structure, binding sites and…

PDB: 6FYL
Type: protein
Length: 340 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dual specificity protein kinase CLK2
EC: 2.7.12.1
UniProt: P49760
Ligands: 3NG
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dual specificity protein kinase CLK2 (EC 2.7.12.1)	protein	340	37% helix, 21% strand	P49760

Ligands and binding sites

3NG · 5-[(3-chlorophenyl)amino]benzo[c][2,6]naphthyridine-8-carboxylic acid · 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	348	0.63	0.78	37	3NG
2	78	0.36	0.76	21	empty

Compared structures

6FYL · X-ray structure of CLK2-KD(136-496)/CX-4945 at 1.95A · the same entry in another collection · chain A against A, TM-score 1.00
P49760 · AlphaFold monomer V2.0 prediction for dual specificity protein kinase CLK2 (P49760) · 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 P49760
Elsewhere: RCSB PDB 6FYL · PDBe 6FYL · UniProt P49760

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.