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Crystal structure of motif N of saccharomyces cerevisiae DBF4

Analyse Crystal structure of motif N of saccharomyces cerevisiae DBF4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OQ0
Type
protein
Length
984 residues
Chains
10
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DBF4
UniProt
P32325
Pockets
12 · best druggability 0.63

Structure

x-ray diffraction · 5 distinct chains · 44% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, FDBF4protein10143% helix, 15% strandP32325
B, GDBF4protein9346% helix, 18% strandP32325
C, HDBF4protein10040% helix, 17% strandP32325
D, IDBF4protein10347% helix, 15% strandP32325
E, JDBF4protein9544% helix, 13% strandP32325

Pockets

12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13300.630.7944empty
22950.600.7946empty
34110.600.7653empty
44140.600.7661empty
51580.520.7924empty

Interfaces

12 interfaces between chains.

  • B–C · 648 Ų buried · 12 hydrogen bonds · protein-protein
  • G–H · 644 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 644 Ų buried · 11 hydrogen bonds · protein-protein
  • H–I · 643 Ų buried · 13 hydrogen bonds · protein-protein
  • F–G · 638 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 modified (engineered).

Compared structures

  • 3OQ0 · Crystal Structure of motif N of Saccharomyces cerevisiae Dbf4 · the same entry in another collection · chain J against J, TM-score 1.00
  • P32325 · AlphaFold monomer V2.0 prediction for ddk kinase regulatory subunit DBF4 (P32325) · a predicted model of the same protein · chain G against A, TM-score 0.98

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