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Mutagenesis of P38 MAP kinase eshtablishes key roles of PHE169 in function and structural dynamics and reveals a novel dfg-out state

Analyse Mutagenesis of P38 MAP kinase eshtablishes key roles of PHE169 in function and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MGY
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 14
EC: 2.7.11.24
UniProt: Q16539
Pockets: 5 · best druggability 0.63

Structure

x-ray diffraction · 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	329	41% helix, 15% strand	Q16539

Ligands and binding sites

BOG · octyl beta-D-glucopyranoside · additive · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	227	0.63	0.82	32	BOG
2	387	0.60	0.76	44	empty
3	91	0.36	0.75	18	empty
4	57	0.35	0.78	17	empty
5	53	0.30	0.75	13	empty

Compared structures

3MGY · Mutagenesis of p38 MAP Kinase eshtablishes key roles of Phe169 in function and structural… · 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 3MGY · PDBe 3MGY · UniProt Q16539

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