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System-wide modulation of hect E3 ligases with selective ubiquitin variant probes: RSP5 and ubv R5.4

Analyse System-wide modulation of hect E3 ligases with selective ubiquitin variant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5HPL
Type
protein
Length
902 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RSP5; Ubiquitin variant R5.4
UniProt
P39940
Pockets
13 · best druggability 0.72

Structure

x-ray diffraction · 3 distinct chains · 46% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARSP5protein37049% helix, 15% strandP39940
BRSP5protein37049% helix, 15% strandP39940
C, DUbiquitin variant R5.4protein8122% helix, 35% strand—

Pockets

13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13980.720.8330empty
28650.710.7688empty
39550.710.7561empty
43070.620.8026empty
53820.620.7834empty

Interfaces

5 interfaces between chains.

  • B–D · 965 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 944 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 508 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 343 Ų buried · 7 hydrogen bonds · protein-protein
  • A–D · 277 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 5HPL · System-wide modulation of HECT E3 ligases with selective ubiquitin variant probes: Rsp5… · the same entry in another collection · chain A against A, TM-score 1.00
  • P39940 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RSP5 (P39940) · a predicted model of the same protein · chain A against A, TM-score 0.98

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