Research workbench
Solution structure of the complex between the SGT2 homodimerization domain and the GET5 ubl domain
Analyse Solution structure of the complex between the SGT2 homodimerization domain and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LXC
- Type
- protein
- Length
- 229 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-like protein MDY2; Small glutamine-rich tetratricopeptide repeat-containing…
- UniProt
- Q12285, Q12118
- Pockets
- 1 · best druggability 0.58
Structure
solution nmr · 2 distinct chains · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin-like protein MDY2 | protein | 81 | 21% helix, 36% strand | Q12285 |
| B, C | Small glutamine-rich tetratricopeptide repeat-containing protein 2 | protein | 74 | 55% helix, 0% strand | Q12118 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.58 | 0.82 | 26 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1574 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 415 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 370 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2LXC · Solution structure of the complex between the Sgt2 homodimerization domain and the Get5… · the same entry in another collection · chain B against B, TM-score 1.00
- Q12285 · AlphaFold monomer V2.0 prediction for ubiquitin-like protein MDY2 (Q12285) · a predicted model of the same protein · chain A against A, TM-score 0.85
- Q12118 · AlphaFold monomer V2.0 prediction for small glutamine-rich tetratricopeptide… · a predicted model of the same protein · chain B against A, TM-score 0.69
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 Q12285
- Every structure of UniProt Q12118
- Elsewhere: RCSB PDB 2LXC · PDBe 2LXC · UniProt Q12285 · UniProt Q12118
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