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Structure of human MNK2 kinase domain mutant D228G

Analyse Structure of human MNK2 kinase domain mutant D228G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AC5
Type: protein
Length: 276 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MAP kinase-interacting SERINE/THREONINE kinase 2
EC: 2.7.1.37
UniProt: Q9HBH9
Ligands: ZN
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MAP kinase-interacting SERINE/THREONINE kinase 2 (EC 2.7.1.37)	protein	276	38% helix, 17% strand	Q9HBH9

Ligands and binding sites

ZN · Zinc ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	397	0.68	0.81	42	empty
2	59	0.47	0.84	13	empty
3	118	0.37	0.73	25	empty

Compared structures

2AC5 · Structure of human Mnk2 Kinase Domain mutant D228G · the same entry in another collection · chain A against A, TM-score 1.00
Q9HBH9 · AlphaFold monomer V2.0 prediction for MAP kinase-interacting SERINE/THREONINE-protein… · a predicted model of the same protein · chain A against A, TM-score 0.88

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 Q9HBH9
Elsewhere: RCSB PDB 2AC5 · PDBe 2AC5 · UniProt Q9HBH9

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