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Crystal structure of ERK2 G169D mutant

Analyse Crystal structure of ERK2 G169D mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6D5Y
Type
protein
Length
337 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
Pockets
4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMitogen-activated protein kinase 1 (EC 2.7.11.24)protein33736% helix, 14% strandP28482

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12820.610.7933empty
2740.480.8319empty
31320.440.7721empty
4510.280.7412empty

Compared structures

  • 6D5Y · Crystal structure of ERK2 G169D mutant · the same entry in another collection · chain A against A, TM-score 1.00

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