Research workbench
S. cerevisiae UBC12
Analyse S. cerevisiae UBC12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O2U
- Type
- protein
- Length
- 375 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NEDD8-conjugating enzyme UBC12
- EC
- 6.3.2.-
- UniProt
- P52491
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NEDD8-conjugating enzyme UBC12 (EC 6.3.2.-) | protein | 190 | 35% helix, 17% strand | P52491 |
| B | NEDD8-conjugating enzyme UBC12 (EC 6.3.2.-) | protein | 185 | 35% helix, 17% strand | P52491 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 508 | 0.69 | 0.80 | 47 | empty |
| 2 | 192 | 0.54 | 0.79 | 22 | GOL |
| 3 | 142 | 0.46 | 0.77 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 839 Ų buried · 10 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 P52491
- Elsewhere: RCSB PDB 3O2U · PDBe 3O2U · UniProt P52491
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