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Structural insights into NEDD8 activation of cullin-ring ligases: conformational control of conjugation.

Analyse Structural insights into NEDD8 activation of cullin-ring ligases… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3DPL
Type
protein
Length
465 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cullin-5; Ring-box protein 1
UniProt
Q93034, P62877
Ligands
ZN
Pockets
6 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CCullin-5protein37852% helix, 16% strandQ93034
RRing-box protein 1protein8714% helix, 30% strandP62877

Ligands and binding sites

  • ZN · Zinc ion · metal · 3 copies · chains R

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16250.750.8162empty
22800.690.8425empty
33250.560.7532ZN
41590.480.7729empty
5790.390.7820empty

Interfaces

1 interface between chains.

  • C–R · 2412 Ų buried · 42 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 3DPL · Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control… · the same entry in another collection · chain C against C, TM-score 1.00
  • Q93034 · AlphaFold monomer V2.0 prediction for cullin-5 (Q93034) · a predicted model of the same protein · chain C against A, TM-score 0.93
  • P62877 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RBX1 (P62877) · a predicted model of the same protein · chain R against A, TM-score 0.76

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