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Cryo-EM structure of the DDB1-DCAF1-CUL4A-RBX1 complex

Analyse Cryo-EM structure of the DDB1-DCAF1-CUL4A-RBX1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OKQ
Type
protein
Length
9,028 residues
Chains
16
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA damage-binding protein 1; DDB1- and CUL4-associated factor 1; Cullin-4A; E3…
EC
2.7.11.1, 2.3.2.27, 2.3.2.32
UniProt
Q16531, Q9Y4B6, Q13619, P62877
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 4 distinct chains · 24% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, E, I, MDNA damage-binding protein 1protein11356% helix, 53% strandQ16531
B, F, J, NDDB1- and CUL4-associated factor 1 (EC 2.7.11.1)protein3317% helix, 45% strandQ9Y4B6
C, G, K, OCullin-4Aprotein71962% helix, 7% strandQ13619
D, H, L, PE3 ubiquitin-protein ligase RBX1 (EC 2.3.2.27, 2.3.2.32)protein7211% helix, 29% strandP62877

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110110.850.87170empty
28910.820.84134empty
39400.820.84136empty
46770.810.86119empty
510840.810.83149empty

Interfaces

24 interfaces between chains.

  • O–P · 1108 Ų buried · 28 hydrogen bonds · protein-protein
  • C–D · 1105 Ų buried · 28 hydrogen bonds · protein-protein
  • G–H · 1105 Ų buried · 28 hydrogen bonds · protein-protein
  • K–L · 1104 Ų buried · 28 hydrogen bonds · protein-protein
  • M–O · 632 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 7OKQ · Cryo-EM Structure of the DDB1-DCAF1-CUL4A-RBX1 Complex · the same entry in another collection · chain K against K, TM-score 1.00

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