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Crystal structure of TRIM7 bound to 2C

Analyse Crystal structure of TRIM7 bound to 2C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7Y3A
Type
protein
Length
540 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase TRIM7,E3 ubiquitin-protein ligase TRIM7,E3 ubiquitin-protein…
EC
2.3.2.27
UniProt
Q9C029
Pockets
6 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CE3 ubiquitin-protein ligase TRIM7,E3 ubiquitin-protein ligase TRIM7,E3 ubiquitin-protein ligase TRIM7,TRIM7-2C (EC 2.3.2.27)protein1812% helix, 40% strandQ9C029
BE3 ubiquitin-protein ligase TRIM7,E3 ubiquitin-protein ligase TRIM7,E3 ubiquitin-protein ligase TRIM7,TRIM7-2C (EC 2.3.2.27)protein1784% helix, 42% strandQ9C029

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11560.560.8132empty
21190.520.8221empty
3500.390.8115empty
4970.380.7619empty
5740.320.7518empty

Interfaces

2 interfaces between chains.

  • A–B · 717 Ų buried · 16 hydrogen bonds · protein-protein
  • A–C · 696 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 7Y3A · Crystal structure of TRIM7 bound to 2C · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9C029 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM7 (Q9C029) · a predicted model of the same protein · chain B against A, TM-score 0.93

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