MolNFT v1 · #92031 · protein

Crystal structure of the ERK2 complexed with EK2

4FUY · Mitogen-activated protein kinase 1: “Crystal structure of the ERK2 complexed with EK2”. X-ray diffraction, 2 ligands (EK2, SO4), 4 pockets (best druggability 0.67). MolNFT v1 #92031 on GenesisL1: 3D structure, binding sites and…

PDB: 4FUY
Type: protein
Length: 332 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: EK2, SO4
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 1 (EC 2.7.11.24)	protein	332	39% helix, 14% strand	P28482

Ligands and binding sites

EK2 · {4-[4-(3,5-dichlorophenyl)-1H-pyrazol-5-yl]-1H-pyrrol-2-yl}(morpholin-4-yl)methanone · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · 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	267	0.67	0.83	35	EK2
2	118	0.53	0.82	28	empty
3	62	0.35	0.77	14	empty
4	63	0.31	0.75	16	empty

Modifications

Observed in the structure: 3 modified (artifact).

Compared structures

4FUY · Crystal Structure of the ERK2 complexed with EK2 · 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 4FUY · PDBe 4FUY · UniProt P28482

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