Research workbench
Light-regulation of imidazole glycerol phosphate synthase by interference with its allosteric machinery through photo-sensitive unnatural amino acids
Analyse Light-regulation of imidazole glycerol phosphate synthase by interference with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RU0
- Type
- protein
- Length
- 1,358 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Imidazole glycerol phosphate synthase subunit hisf; Imidazole glycerol phosphate synthase…
- EC
- 4.3.2.10, 3.5.1.2
- UniProt
- Q9X0C6, Q9X0C8
- Ligands
- PO4
- Pockets
- 13 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | Imidazole glycerol phosphate synthase subunit hisf (EC 4.3.2.10) | protein | 253 | 37% helix, 25% strand | Q9X0C6 |
| B, D | Imidazole glycerol phosphate synthase subunit hish (EC 4.3.2.10, 3.5.1.2) | protein | 200 | 27% helix, 34% strand | Q9X0C8 |
| F | Imidazole glycerol phosphate synthase subunit hish (EC 4.3.2.10, 3.5.1.2) | protein | 199 | 27% helix, 34% strand | Q9X0C8 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains A, C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 584 | 0.75 | 0.82 | 67 | empty |
| 2 | 520 | 0.74 | 0.82 | 64 | empty |
| 3 | 311 | 0.67 | 0.82 | 36 | empty |
| 4 | 568 | 0.66 | 0.77 | 67 | empty |
| 5 | 386 | 0.66 | 0.79 | 48 | PO4 |
Interfaces
6 interfaces between chains.
- A–B · 1135 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1095 Ų buried · 17 hydrogen bonds · protein-protein
- E–F · 1053 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 537 Ų buried · 5 hydrogen bonds · protein-protein
- D–E · 171 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6RU0 · Light-Regulation of Imidazole Glycerol Phosphate Synthase by Interference with its… · the same entry in another collection · chain F against F, TM-score 1.00
- Q9X0C8 · AlphaFold monomer V2.0 prediction for imidazole glycerol phosphate synthase subunit hish… · a predicted model of the same protein · chain F against A, TM-score 0.99
- Q9X0C6 · AlphaFold monomer V2.0 prediction for imidazole glycerol phosphate synthase subunit hisf… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9X0C6
- Every structure of UniProt Q9X0C8
- Elsewhere: RCSB PDB 6RU0 · PDBe 6RU0 · UniProt Q9X0C6 · UniProt Q9X0C8
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