Research workbench
Cryo-EM structure of ultraviolet-B activated UVR8 in complex with COP1
Analyse Cryo-EM structure of ultraviolet-B activated UVR8 in complex with COP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VGG
- Type
- protein
- Length
- 680 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase COP1; Ultraviolet-B receptor UVR8
- EC
- 2.3.2.27
- UniProt
- P43254, Q9FN03
- Pockets
- 5 · best druggability 0.77
Structure
electron microscopy · 2 distinct chains · 4% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase COP1 (EC 2.3.2.27) | protein | 304 | 2% helix, 53% strand | P43254 |
| B | Ultraviolet-B receptor UVR8 | protein | 376 | 5% helix, 42% strand | Q9FN03 |
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.77 | 0.86 | 50 | empty |
| 2 | 98 | 0.76 | 0.97 | 29 | empty |
| 3 | 485 | 0.75 | 0.84 | 46 | empty |
| 4 | 484 | 0.68 | 0.79 | 57 | empty |
| 5 | 132 | 0.51 | 0.80 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1509 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 7VGG · Cryo-EM structure of Ultraviolet-B activated UVR8 in complex with COP1 · the same entry in another collection · chain A against A, TM-score 1.00
- P43254 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase COP1 (P43254) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q9FN03 · AlphaFold monomer V2.0 prediction for ultraviolet-B receptor UVR8 (Q9FN03) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P43254
- Every structure of UniProt Q9FN03
- Elsewhere: RCSB PDB 7VGG · PDBe 7VGG · UniProt P43254 · UniProt Q9FN03
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