MolNFT v1 · #71102 · protein

Crystal structure of mapkap kinase 2 (MK2) complexed with a tetracyclic ATP site inhibitor

3M42 · MAP kinase-activated protein kinase 2: “Crystal structure of mapkap kinase 2 (MK2) complexed with a tetracyclic ATP site inhibitor”. X-ray diffraction, 2 ligands (HGF, MG), 4 pockets (best druggability 0.64). MolNFT v1 #71102 on…

PDB: 3M42
Type: protein
Length: 290 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MAP kinase-activated protein kinase 2
EC: 2.7.11.1
UniProt: P49137
Ligands: HGF, MG
Pockets: 4 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MAP kinase-activated protein kinase 2 (EC 2.7.11.1)	protein	290	40% helix, 21% strand	P49137

Ligands and binding sites

HGF · 2-[5-(2-methoxyethoxy)pyridin-3-yl]-8,9,10,11-tetrahydro-7H-pyrido[3',4':4,5]pyrrolo[2,3-f]isoquinolin-7-one · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

4 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	180	0.64	0.84	29	HGF
2	79	0.56	0.86	19	empty
3	89	0.35	0.74	18	empty
4	76	0.32	0.74	17	empty

Compared structures

3M42 · Crystal structure of MAPKAP kinase 2 (MK2) complexed with a tetracyclic ATP site inhibitor · 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 P49137
Elsewhere: RCSB PDB 3M42 · PDBe 3M42 · UniProt P49137

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