Research workbench
Structure of a putative glutamine--fructose-6-phosphate aminotransferase from staphylococcus aureus subsp. aureus MU50
Analyse Structure of a putative glutamine--fructose-6-phosphate aminotransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4S1W
- Type
- protein
- Length
- 679 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
- EC
- 2.6.1.16
- UniProt
- A0A060U032
- Pockets
- 4 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (EC 2.6.1.16) | protein | 336 | 51% helix, 17% strand | A0A060U032 |
| B | Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (EC 2.6.1.16) | protein | 343 | 50% helix, 17% strand | A0A060U032 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1160 | 0.87 | 0.87 | 75 | empty |
| 2 | 223 | 0.53 | 0.77 | 37 | empty |
| 3 | 173 | 0.47 | 0.76 | 32 | empty |
| 4 | 54 | 0.27 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1923 Ų buried · 34 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 4S1W · Structure of a putative Glutamine--Fructose-6-Phosphate Aminotransferase from… · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A060U032
- Elsewhere: RCSB PDB 4S1W · PDBe 4S1W · UniProt A0A060U032
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