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Human STK10 bound to GW683134A

Analyse Human STK10 bound to GW683134A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EIM
Type: protein
Length: 581 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.43
Source: Homo sapiens
Molecule: Serine/threonine-protein kinase 10
EC: 2.7.11.1
UniProt: O94804
Ligands: B6E
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · resolution 1.43 · 2 distinct chains · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine/threonine-protein kinase 10 (EC 2.7.11.1)	protein	286	45% helix, 15% strand	O94804
B	Serine/threonine-protein kinase 10 (EC 2.7.11.1)	protein	295	43% helix, 15% strand	O94804

Ligands and binding sites

B6E · ~{N}-[5-[4-[[2-fluoranyl-5-(trifluoromethyl) phenyl]carbamoylamino]phenoxy]-1~{H}-benzimidazol-2-yl]furan-2-carboxamide · ligand · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 5 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	318	0.77	0.89	41	empty
2	478	0.74	0.83	59	B6E
3	200	0.72	0.88	32	B6E
4	96	0.34	0.73	21	empty
5	70	0.31	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 2103 Å² buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6EIM · Human STK10 bound to GW683134A · the same entry in another collection · chain A against A, TM-score 1.00
O94804 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase 10 (O94804) · a predicted model of the same protein · chain A against A, TM-score 0.87

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 O94804
Elsewhere: RCSB PDB 6EIM · PDBe 6EIM · UniProt O94804

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