MolNFT v1 · #149370 · protein

X-ray structure of CLK2-KD(130-496)/TG003 at 2.6A

6FYI · Dual specificity protein kinase CLK2: “X-ray structure of CLK2-KD(130-496)/TG003 at 2.6A”. X-ray diffraction, 1 ligand (EAE), 2 pockets (best druggability 0.64). MolNFT v1 #149370 on GenesisL1: 3D structure, binding sites and…

PDB: 6FYI
Type: protein
Length: 336 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: EAE
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dual specificity protein kinase CLK2 (EC 2.7.12.1)	protein	336	38% helix, 21% strand	P49760

Ligands and binding sites

EAE · (1~{Z})-1-(3-ethyl-5-methoxy-1,3-benzothiazol-2-ylidene)propan-2-one · 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	332	0.64	0.79	33	EAE
2	92	0.35	0.75	17	empty

Compared structures

6FYI · X-ray Structure of CLK2-KD(130-496)/TG003 at 2.6A · 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 6FYI · PDBe 6FYI · UniProt P49760

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