MolNFT v1 · #92394 · protein

Crystal structure of the ERK2

4G6N · Mitogen-activated protein kinase 1: “Crystal structure of the ERK2”. X-ray diffraction, 2 ligands (EK0, SO4), 4 pockets (best druggability 0.68). MolNFT v1 #92394 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4G6N
Type: protein
Length: 342 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 1
EC: 2.7.11.24
UniProt: P28482
Ligands: EK0, SO4
Pockets: 4 · best druggability 0.68

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 1 (EC 2.7.11.24)	protein	342	39% helix, 15% strand	P28482

Ligands and binding sites

EK0 · 3-(4-chlorophenyl)-4,5,6,7-tetrahydro-1H-indazole · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · 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	360	0.68	0.81	36	EK0
2	123	0.54	0.82	29	empty
3	87	0.33	0.74	15	empty
4	65	0.31	0.75	14	empty

Modifications

Observed in the structure: 1 modified (artifact).

Compared structures

4G6N · Crystal Structure of the ERK2 · 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 P28482
Elsewhere: RCSB PDB 4G6N · PDBe 4G6N · UniProt P28482

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.