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Structure of MAPK14 with bound the kim domain of the toxoplasma protein GRA24

Analyse Structure of MAPK14 with bound the kim domain of the toxoplasma protein GRA24 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ETA
Type
protein
Length
703 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mitogen-activated protein kinase 14; Putative transmembrane protein
EC
2.7.11.24
UniProt
Q16539, A0A086L2F3
Pockets
13 · best druggability 0.68

Structure

x-ray diffraction · 3 distinct chains · 40% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BMitogen-activated protein kinase 14 (EC 2.7.11.24)protein33540% helix, 16% strandQ16539
D, CPutative transmembrane proteinprotein1625% helix, 0% strandA0A086L2F3
AMitogen-activated protein kinase 14 (EC 2.7.11.24)protein33641% helix, 16% strandQ16539

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14690.680.7962empty
23550.640.7944empty
3670.620.9016empty
42120.520.7733empty
51920.490.7626empty

Interfaces

6 interfaces between chains.

  • A–C · 838 Ų buried · 11 hydrogen bonds · protein-protein
  • B–D · 808 Ų buried · 14 hydrogen bonds · protein-protein
  • B–A · 215 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 56 Ų buried · 0 hydrogen bonds · protein-protein
  • D–C · 52 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 5ETA · Structure of MAPK14 with bound the KIM domain of the Toxoplasma protein GRA24 · the same entry in another collection · chain B against B, TM-score 1.00

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