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Crystal structure of the ERK2 complexed with EK7

Analyse Crystal structure of the ERK2 complexed with EK7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FV4
Type: protein
Length: 330 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: EK7, SO4
Pockets: 4 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 1 (EC 2.7.11.24)	protein	330	40% helix, 15% strand	P28482

Ligands and binding sites

EK7 · 9-(dimethylamino)-2-[(3-hydroxyphenyl)amino]-5,6-dihydrothieno[3,4-h]quinazoline-7-carbonitrile · ligand · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A
GOL · Glycerol · additive · 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	214	0.62	0.82	24	EK7
2	140	0.51	0.79	15	empty
3	103	0.49	0.81	29	empty
4	52	0.30	0.76	17	empty

Modifications

Observed in the structure: 1 modified (artifact).

Compared structures

4FV4 · Crystal Structure of the ERK2 complexed with EK7 · 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 4FV4 · PDBe 4FV4 · UniProt P28482

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