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Crystal structure of nhl domain of TRIM2 (full C-terminal)

Analyse Crystal structure of nhl domain of TRIM2 (full C-terminal) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7QRV
Type
protein
Length
1,113 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tripartite motif-containing protein 2
EC
2.3.2.27
UniProt
Q9C040
Pockets
10 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 2% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CTripartite motif-containing protein 2 (EC 2.3.2.27)protein2782% helix, 49% strandQ9C040
BTripartite motif-containing protein 2 (EC 2.3.2.27)protein2762% helix, 49% strandQ9C040
DTripartite motif-containing protein 2 (EC 2.3.2.27)protein2812% helix, 48% strandQ9C040

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 26 copies · chains A, C, D, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110760.820.8373EDO
29640.800.8168EDO
33820.670.8046EDO
43500.660.8037EDO
53460.650.8036EDO

Interfaces

4 interfaces between chains.

  • A–D · 719 Ų buried · 9 hydrogen bonds · protein-protein
  • B–C · 667 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 240 Ų buried · 1 hydrogen bond · protein-protein
  • B–D · 141 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 7QRV · Crystal structure of NHL domain of TRIM2 (full C-terminal) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9C040 · AlphaFold monomer V2.0 prediction for tripartite motif-containing protein 2 (Q9C040) · a predicted model of the same protein · chain B against A, TM-score 0.99

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