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Structure of penta mutant human ERK2 MAP kinase complexed with a specific inhibitor of human P38 MAP kinase

Analyse Structure of penta mutant human ERK2 MAP kinase complexed with a specific… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PME
Type: protein
Length: 334 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ERK2
EC: 2.7.1.-
UniProt: P28482
Ligands: SB2, SO4
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ERK2 (EC 2.7.1.-)	protein	334	40% helix, 13% strand	P28482

Ligands and binding sites

SB2 · 4-[5-(4-fluoro-phenyl)-2-(4-methanesulfinyl-phenyl)-3H-imidazol-4-yl]-pyridine · ligand · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

3 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	313	0.63	0.80	36	SB2
2	93	0.51	0.83	17	empty
3	54	0.28	0.73	11	empty

Modifications

Observed in the structure: 1 modified (artifact).

Compared structures

1PME · Structure of penta mutant human ERK2 MAP kinase complexed with a specific inhibitor of… · 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 1PME · PDBe 1PME · UniProt P28482

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