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Crystal structure of P38 alpha in complex with DP802

Analyse Crystal structure of P38 alpha in complex with DP802 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NNW
Type: protein
Length: 349 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.89
Source: Homo sapiens
Molecule: Mitogen-activated protein kinase 14
EC: 2.7.11.24
UniProt: Q16539
Ligands: EDD
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · resolution 1.89 · 1 distinct chain · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	349	41% helix, 15% strand	Q16539

Ligands and binding sites

EDD · 2-[3-(3-tert-butyl-5-{[(2,3-dichlorophenyl)carbamoyl]imino}-2,5-dihydro-1H-pyrazol-1-yl)phenyl]acetamide · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	455	0.76	0.85	47	EDD
2	147	0.44	0.75	24	empty
3	55	0.30	0.76	18	empty
4	64	0.29	0.74	15	empty
5	53	0.27	0.74	15	empty

Compared structures

3NNW · Crystal structure of P38 alpha in complex with DP802 · 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 3NNW · PDBe 3NNW · UniProt Q16539

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