Research workbench
Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.
Analyse Molecular basis for the unique allosteric activation mechanism of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AC8
- Type
- protein
- Length
- 1,356 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
- GLN, GUO, PO4
- Pockets
- 17 · best druggability 0.82
Structure
x-ray diffraction · 5 distinct chains · 33% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Imidazole glycerol phosphate synthase subunit hisf (EC 4.3.2.10) | protein | 252 | 39% helix, 24% strand | Q9X0C6 |
| B | Imidazole glycerol phosphate synthase subunit hish (EC 4.3.2.10, 3.5.1.2) | protein | 202 | 28% helix, 33% strand | Q9X0C8 |
| D | Imidazole glycerol phosphate synthase subunit hish (EC 4.3.2.10, 3.5.1.2) | protein | 201 | 28% helix, 33% strand | Q9X0C8 |
| E | Imidazole glycerol phosphate synthase subunit hisf (EC 4.3.2.10) | protein | 251 | 36% helix, 29% strand | Q9X0C6 |
| F | Imidazole glycerol phosphate synthase subunit hish (EC 4.3.2.10, 3.5.1.2) | protein | 198 | 29% helix, 33% strand | Q9X0C8 |
Ligands and binding sites
- GLN · Glutamine · ligand · 3 copies · chains A, B, C, D, E, F
- GUO · [(2R,3S,4R,5R)-5-[4-aminocarbonyl-5-[(E)-[[(2R,3R,4S, 5R)-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]amino]methylideneamino]imidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate · ligand · 2 copies · chains A, E
- PO4 · Phosphate ion · ion · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 250 | 0.82 | 0.94 | 51 | GUO |
| 2 | 591 | 0.72 | 0.80 | 60 | GLN |
| 3 | 371 | 0.70 | 0.82 | 48 | GLN |
| 4 | 402 | 0.64 | 0.78 | 45 | PO4 |
| 5 | 353 | 0.64 | 0.79 | 39 | GUO |
Interfaces
7 interfaces between chains.
- E–F · 1549 Ų buried · 32 hydrogen bonds · protein-protein
- C–D · 1171 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1161 Ų buried · 21 hydrogen bonds · protein-protein
- C–E · 582 Ų buried · 8 hydrogen bonds · protein-protein
- A–F · 550 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 7AC8 · Molecular basis for the unique allosteric activation mechanism of the heterodimeric… · 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 C 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 7AC8 · PDBe 7AC8 · UniProt Q9X0C6 · UniProt Q9X0C8
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