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The structure of ERK2 in complex with a small molecule inhibitor

Analyse The structure of ERK2 in complex with a small molecule inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TVO
Type: protein
Length: 350 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 1
EC: 2.7.1.37
UniProt: P28482
Ligands: FRZ
Pockets: 5 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 1 (EC 2.7.1.37)	protein	350	37% helix, 14% strand	P28482

Ligands and binding sites

FRZ · 5-(2-phenylpyrazolo[1,5-a]pyridin-3-yl)-1H-pyrazolo[3, 4-c]pyridazin-3-amine · ligand · 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	381	0.69	0.81	34	FRZ
2	156	0.52	0.79	31	empty
3	68	0.42	0.81	20	empty
4	108	0.40	0.76	19	empty
5	53	0.29	0.75	12	empty

Compared structures

1TVO · The structure of ERK2 in complex with a small molecule 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 P28482
Elsewhere: RCSB PDB 1TVO · PDBe 1TVO · UniProt P28482

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