MolNFT v1 · #71534 · protein

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

3MH2 · Mitogen-activated protein kinase 14: “Mutagenesis of P38 MAP kinase establishes key roles of PHE169 in function and structural dynamics and reveals…”. X-ray diffraction, 5 pockets (best druggability 0.62). MolNFT v1 #71534 on…

PDB: 3MH2
Type: protein
Length: 330 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 0.62

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	330	39% 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	320	0.62	0.79	38	empty
2	107	0.61	0.87	20	BOG
3	95	0.38	0.75	17	empty
4	93	0.37	0.75	26	empty
5	57	0.29	0.74	14	empty

Compared structures

3MH2 · Mutagenesis of p38 MAP kinase establishes 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 3MH2 · PDBe 3MH2 · UniProt Q16539

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