MolNFT v1 · #172744 · protein
Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.
7AC8 · Imidazole glycerol phosphate synthase subunit hisf: “Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol…”. X-ray diffraction, 3 ligands (GLN, GUO, PO4), 17 pockets (best…
- 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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