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Discovery of 5,6,7,8-TETRAHYDROPYRIDO[3,4-D]PYRIMIDINE inhibitors of ERK2

Analyse Discovery of 5,6,7,8-TETRAHYDROPYRIDO[3,4-D]PYRIMIDINE inhibitors of ERK2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4O6E
Type: protein
Length: 328 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: 2SH
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 1 (EC 2.7.11.24)	protein	328	41% helix, 15% strand	P28482

Ligands and binding sites

2SH · N-[(1S)-1-(3-chloro-4-fluorophenyl)-2-hydroxyethyl]-2-(tetrahydro-2H-pyran-4-ylamino)-5,8-dihydropyrido[3,4-d]pyrimidine-7(6H)-carboxamide · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	429	0.69	0.80	39	2SH
2	64	0.48	0.84	15	empty
3	54	0.38	0.80	16	empty
4	55	0.29	0.75	16	empty

Compared structures

4O6E · Discovery of 5,6,7,8-tetrahydropyrido[3,4-d]pyrimidine Inhibitors of 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 4O6E · PDBe 4O6E · UniProt P28482

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