Research workbench
Staphylococcus aureus monofunctional glycosyltransferase in complex with moenomycin
Analyse Staphylococcus aureus monofunctional glycosyltransferase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FTB
- Type
- protein
- Length
- 210 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Monofunctional glycosyltransferase
- EC
- 2.4.1.129
- UniProt
- Q7A0I6
- Ligands
- M0E, 1QW, PO4
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Monofunctional glycosyltransferase (EC 2.4.1.129) | protein | 210 | 55% helix, 3% strand | Q7A0I6 |
Ligands and binding sites
- M0E · Moenomycin · ligand · 3 copies · chains A
- 1QW · (2R)-2,3-dihydroxypropyl dodecanoate · ligand · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 8 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 134 | 0.43 | 0.76 | 25 | EDO |
| 2 | 56 | 0.36 | 0.79 | 18 | M0E |
Compared structures
- 6FTB · Staphylococcus aureus monofunctional glycosyltransferase in complex with moenomycin · the same entry in another collection · chain A against A, TM-score 1.00
- Q7A0I6 · AlphaFold monomer V2.0 prediction for monofunctional glycosyltransferase (Q7A0I6) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q7A0I6
- Elsewhere: RCSB PDB 6FTB · PDBe 6FTB · UniProt Q7A0I6
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