Research workbench
TRIM23 ring domain
Analyse TRIM23 ring domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VZV
- Type
- protein
- Length
- 230 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase TRIM23
- EC
- 2.3.2.27
- UniProt
- P36406
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | E3 ubiquitin-protein ligase TRIM23 (EC 2.3.2.27) | protein | 77 | 27% helix, 22% strand | P36406 |
| B | E3 ubiquitin-protein ligase TRIM23 (EC 2.3.2.27) | protein | 76 | 25% helix, 21% strand | P36406 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 430 | 0.73 | 0.83 | 48 | empty |
| 2 | 92 | 0.47 | 0.81 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–C · 826 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 258 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 228 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P36406
- Elsewhere: RCSB PDB 5VZV · PDBe 5VZV · UniProt P36406
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