MolNFT v1 · #112848 · protein

Complex of ERK2 with catechol

4ZXT · Mitogen-activated protein kinase 1: “Complex of ERK2 with catechol”. X-ray diffraction, 3 ligands (CAQ, SO4, NH4), 4 pockets (best druggability 0.64). MolNFT v1 #112848 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4ZXT
Type: protein
Length: 351 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: CAQ, SO4, NH4
Pockets: 4 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 1 (EC 2.7.11.24)	protein	351	40% helix, 14% strand	P28482

Ligands and binding sites

CAQ · Catechol · ligand · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A
NH4 · Ammonium ion · ion · 2 copies · 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	273	0.64	0.81	39	CAQ
2	87	0.50	0.83	18	empty
3	55	0.31	0.76	12	NH4
4	59	0.31	0.75	18	empty

Modifications

Observed in the structure: 3 modified (artifact).

Compared structures

4ZXT · Complex of ERK2 with catechol · 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 4ZXT · PDBe 4ZXT · UniProt P28482

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