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The LIMK1 kinase domain bound to LIJTF500127

Analyse The LIMK1 kinase domain bound to LIJTF500127 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ATS
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lim domain kinase 1
EC: 2.7.11.1
UniProt: P53667
Ligands: RXQ
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lim domain kinase 1 (EC 2.7.11.1)	protein	275	41% helix, 18% strand	P53667

Ligands and binding sites

RXQ · N-[3-[5-(4-Chlorophenyl)-1H-pyrrolo[2,3-b]pyridine-3-carbonyl]-2,4-difluorophenyl]benzenesulfonamide · ligand · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	395	0.70	0.82	41	RXQ
2	101	0.61	0.87	26	empty
3	56	0.28	0.74	16	empty

Compared structures

7ATS · The LIMK1 Kinase Domain Bound To LIJTF500127 · the same entry in another collection · chain A against A, TM-score 1.00
P53667 · AlphaFold monomer V2.0 prediction for lim domain kinase 1 (P53667) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P53667
Elsewhere: RCSB PDB 7ATS · PDBe 7ATS · UniProt P53667

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