Research workbench
Crystal structure of plant uvb photoreceptor UVR8 from in situ serial laue diffraction
Analyse Crystal structure of plant uvb photoreceptor UVR8 from in situ serial laue… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DD7
- Type
- protein
- Length
- 1,472 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ultraviolet-B receptor UVR8
- UniProt
- Q9FN03
- Pockets
- 12 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Ultraviolet-B receptor UVR8 | protein | 368 | 4% helix, 43% strand | Q9FN03 |
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 440 | 0.85 | 0.93 | 46 | empty |
| 2 | 503 | 0.85 | 0.91 | 55 | empty |
| 3 | 468 | 0.75 | 0.84 | 46 | empty |
| 4 | 469 | 0.75 | 0.84 | 46 | empty |
| 5 | 443 | 0.74 | 0.84 | 45 | empty |
Interfaces
4 interfaces between chains.
- B–C · 1511 Ų buried · 40 hydrogen bonds · protein-protein
- A–D · 1503 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 275 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 46 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6DD7 · Crystal structure of plant UVB photoreceptor UVR8 from in situ serial Laue diffraction · the same entry in another collection · chain A against A, TM-score 1.00
- Q9FN03 · AlphaFold monomer V2.0 prediction for ultraviolet-B receptor UVR8 (Q9FN03) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q9FN03
- Elsewhere: RCSB PDB 6DD7 · PDBe 6DD7 · UniProt Q9FN03
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