Research workbench
Crystal structure of UBE2G2 in complex with the UBE2G2-binding region of AUP1
Analyse Crystal structure of UBE2G2 in complex with the UBE2G2-binding region of AUP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LEW
- Type
- protein
- Length
- 182 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-conjugating enzyme E2 G2; Lipid droplet-regulating vldl assembly factor AUP1
- EC
- 2.3.2.23
- UniProt
- P60604, Q9Y679
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin-conjugating enzyme E2 G2 (EC 2.3.2.23) | protein | 154 | 36% helix, 17% strand | P60604 |
| B | Lipid droplet-regulating vldl assembly factor AUP1 | protein | 28 | 86% helix, 0% strand | Q9Y679 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.33 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 943 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7LEW · Crystal structure of UBE2G2 in complex with the UBE2G2-binding region of AUP1 · the same entry in another collection · chain A against A, TM-score 1.00
- P60604 · AlphaFold monomer V2.0 prediction for ubiquitin-conjugating enzyme E2 G2 (P60604) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q9Y679 · AlphaFold monomer V2.0 prediction for lipid droplet-regulating vldl assembly factor AUP1… · a predicted model of the same protein · chain B against A, TM-score 0.83
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 P60604
- Every structure of UniProt Q9Y679
- Elsewhere: RCSB PDB 7LEW · PDBe 7LEW · UniProt P60604 · UniProt Q9Y679
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