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CDC48-NPL4 complex in the presence of ATP-gamma-S

Analyse CDC48-NPL4 complex in the presence of ATP-gamma-S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6CHS
Type
protein
Length
3,760 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NPL4; Putative cell division control protein
UniProt
G0S0B4, G0S6Y2
Ligands
AGS, MG, ZN
Pockets
20 · best druggability 0.83

Structure

electron microscopy · 2 distinct chains · 38% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANPL4protein46025% helix, 18% strandG0S0B4
H, I, J, D, E, FPutative cell division control proteinprotein55048% helix, 10% strandG0S6Y2

Ligands and binding sites

  • AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 12 copies · chains H, F, I, J, D, E
  • MG · Magnesium ion · metal · 12 copies · chains H, I, J, D, E, F
  • ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17510.830.86111AGS, MG
210340.830.84109empty
37120.830.87106AGS, MG
410730.820.83118AGS, MG
56400.820.8791empty

Interfaces

12 interfaces between chains.

  • H–I · 3510 Ų buried · 32 hydrogen bonds · protein-protein
  • J–D · 3503 Ų buried · 33 hydrogen bonds · protein-protein
  • E–F · 3501 Ų buried · 35 hydrogen bonds · protein-protein
  • I–J · 3469 Ų buried · 35 hydrogen bonds · protein-protein
  • H–F · 3325 Ų buried · 26 hydrogen bonds · protein-protein

Compared structures

  • 6CHS · Cdc48-Npl4 complex in the presence of ATP-gamma-S · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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