Research workbench
Crystal structure of staphylococcus aureus membrane-bound transglycosylase in complex with nbd-lipid II
Analyse Crystal structure of staphylococcus aureus membrane-bound transglycosylase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VMS
- Type
- protein
- Length
- 437 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Monofunctional glycosyltransferase
- EC
- 2.4.-.-
- UniProt
- Q99T05
- Pockets
- 6 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Monofunctional glycosyltransferase (EC 2.4.-.-) | protein | 220 | 58% helix, 2% strand | Q99T05 |
| B | Monofunctional glycosyltransferase (EC 2.4.-.-) | protein | 217 | 56% helix, 1% strand | Q99T05 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 160 | 0.43 | 0.75 | 22 | empty |
| 2 | 126 | 0.43 | 0.77 | 20 | empty |
| 3 | 77 | 0.41 | 0.80 | 17 | empty |
| 4 | 104 | 0.37 | 0.75 | 24 | empty |
| 5 | 59 | 0.34 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 568 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3VMS · Crystal structure of Staphylococcus aureus membrane-bound transglycosylase in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- Q99T05 · AlphaFold monomer V2.0 prediction for monofunctional glycosyltransferase (Q99T05) · a predicted model of the same protein · chain A 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 Q99T05
- Elsewhere: RCSB PDB 3VMS · PDBe 3VMS · UniProt Q99T05
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