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Crystal structure of rice GID1 complexed with GA4
Analyse Crystal structure of rice GID1 complexed with GA4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EBL
- Type
- protein
- Length
- 1,877 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gibberellin receptor GID1
- EC
- 3.-.-.-
- UniProt
- Q6L545
- Ligands
- GA4, NO3, PO4
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 6 distinct chains · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gibberellin receptor GID1 (EC 3.-.-.-) | protein | 323 | 38% helix, 19% strand | Q6L545 |
| B | Gibberellin receptor GID1 (EC 3.-.-.-) | protein | 318 | 37% helix, 18% strand | Q6L545 |
| C | Gibberellin receptor GID1 (EC 3.-.-.-) | protein | 301 | 40% helix, 19% strand | Q6L545 |
| D | Gibberellin receptor GID1 (EC 3.-.-.-) | protein | 315 | 38% helix, 18% strand | Q6L545 |
| E | Gibberellin receptor GID1 (EC 3.-.-.-) | protein | 315 | 38% helix, 19% strand | Q6L545 |
| F | Gibberellin receptor GID1 (EC 3.-.-.-) | protein | 305 | 39% helix, 19% strand | Q6L545 |
Ligands and binding sites
- GA4 · Gibberellin A4 · ligand · 6 copies · chains A, B, C, D, E, F
- NO3 · Nitrate ion · ion · 18 copies · chains A, B, C, D, E, F
- PO4 · Phosphate ion · ion · 2 copies · chains A, B, E, F
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.84 | 0.96 | 41 | GA4 |
| 2 | 238 | 0.83 | 0.96 | 43 | GA4 |
| 3 | 243 | 0.83 | 0.95 | 43 | GA4 |
| 4 | 246 | 0.83 | 0.95 | 42 | GA4 |
| 5 | 251 | 0.83 | 0.95 | 42 | GA4 |
Interfaces
7 interfaces between chains.
- E–F · 989 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 988 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 959 Ų buried · 7 hydrogen bonds · protein-protein
- B–E · 255 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 255 Ų buried · 0 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 Q6L545
- Elsewhere: RCSB PDB 3EBL · PDBe 3EBL · UniProt Q6L545
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