GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the MK2H_DELTAMIL peptide homodimer

Analyse Crystal structure of the MK2H_DELTAMIL peptide homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DXW
Type
protein
Length
43 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MK2H_DELTAMIL protein
Ligands
SO4
Pockets
1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMK2H_DELTAMIL proteinprotein4323% helix, 0% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12260.490.7427empty

Compared structures

  • 7DXW · Crystal structure of the mk2h_deltaMIL peptide homodimer · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.