MolNFT v1 · #64273 · protein

Crystal structure of a benzthiophene lead bound to mapkap kinase-2 (mk-2)

3FYK · MAP kinase-activated protein kinase 2: “Crystal structure of a benzthiophene lead bound to mapkap kinase-2 (mk-2)”. X-ray diffraction, 1 ligand (B98), 4 pockets (best druggability 0.69). MolNFT v1 #64273 on GenesisL1: 3D structure…

PDB: 3FYK
Type: protein
Length: 282 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: B98
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	MAP kinase-activated protein kinase 2 (EC 2.7.11.1)	protein	282	34% helix, 19% strand	P49137

Ligands and binding sites

B98 · (3R)-3-(aminomethyl)-9-methoxy-1,2,3,4-tetrahydro-5H-[1]benzothieno[3,2-e][1,4]diazepin-5-one · ligand · chains X

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

Pockets

4 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	239	0.69	0.85	35	B98
2	121	0.45	0.77	18	empty
3	96	0.39	0.76	14	empty
4	94	0.36	0.74	22	empty

Compared structures

3FYK · Crystal structure of a benzthiophene lead bound to MAPKAP Kinase-2 (MK-2) · the same entry in another collection · chain X against X, 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 3FYK · PDBe 3FYK · UniProt P49137

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