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Solution structure of human J-protein co-chaperone, DPH4

Analyse Solution structure of human J-protein co-chaperone, DPH4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2L6L
Type
protein
Length
155 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dnaj homolog subfamily C member 24
UniProt
Q6P3W2
Ligands
ZN
Pockets
2 · best druggability 0.36

Structure

solution nmr · 1 distinct chain · 39% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADnaj homolog subfamily C member 24protein15539% helix, 16% strandQ6P3W2

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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11120.360.7414empty
2540.300.7616empty

Compared structures

  • 2L6L · Solution structure of human J-protein co-chaperone, Dph4 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q6P3W2 · AlphaFold monomer V2.0 prediction for dnaj homolog subfamily C member 24 (Q6P3W2) · a predicted model of the same protein · chain A against A, TM-score 0.38

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