Research workbench

p38alpha in complex with pyrazolobenzothiazine inhibitor COXH11

Analyse p38alpha in complex with pyrazolobenzothiazine inhibitor COXH11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OMH
Type: protein
Length: 325 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.5
Source: Homo sapiens
Molecule: Mitogen-activated protein kinase 14
EC: 2.7.11.24
UniProt: Q16539
Ligands: 9Y5
Pockets: 5 · best druggability 0.69

Structure

x-ray diffraction · resolution 2.5 · 1 distinct chain · 39% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	325	39% helix, 14% strand	Q16539

Ligands and binding sites

9Y5 · 1-(3-chlorophenyl)-3-methyl-4~{H}-pyrazolo[4,3-c][1,2]benzothiazine 5,5-dioxide · ligand · chains A

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	167	0.69	0.88	21	empty
2	316	0.60	0.78	45	9Y5
3	188	0.57	0.81	31	empty
4	67	0.31	0.74	16	empty
5	56	0.27	0.73	15	empty

Compared structures

5OMH · P38ALPHA in complex with pyrazolobenzothiazine inhibitor COXH11 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q16539
Elsewhere: RCSB PDB 5OMH · PDBe 5OMH · UniProt Q16539

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