Research workbench
Structure of SYM2 D9V+D55V+D130V+D176V
Analyse Structure of SYM2 D9V+D55V+D130V+D176V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FX7
- Type
- protein
- Length
- 960 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Imidazole glycerol phosphate synthase subunit hisf
- EC
- 4.1.3.-
- UniProt
- Q9X0C6
- Ligands
- PI
- Pockets
- 8 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 39% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Imidazole glycerol phosphate synthase subunit hisf (EC 4.1.3.-) | protein | 240 | 39% helix, 30% strand | Q9X0C6 |
| B | Imidazole glycerol phosphate synthase subunit hisf (EC 4.1.3.-) | protein | 241 | 39% helix, 30% strand | Q9X0C6 |
| C | Imidazole glycerol phosphate synthase subunit hisf (EC 4.1.3.-) | protein | 240 | 37% helix, 30% strand | Q9X0C6 |
| D | Imidazole glycerol phosphate synthase subunit hisf (EC 4.1.3.-) | protein | 239 | 41% helix, 30% strand | Q9X0C6 |
Ligands and binding sites
- PI · Hydrogenphosphate ion · ion · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 976 | 0.85 | 0.86 | 100 | PI |
| 2 | 501 | 0.79 | 0.86 | 64 | PI |
| 3 | 279 | 0.79 | 0.91 | 42 | PI |
| 4 | 314 | 0.79 | 0.90 | 45 | PI |
| 5 | 279 | 0.60 | 0.79 | 28 | empty |
Interfaces
5 interfaces between chains.
- A–B · 455 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 409 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 396 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 171 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 62 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 Q9X0C6
- Elsewhere: RCSB PDB 4FX7 · PDBe 4FX7 · UniProt Q9X0C6
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