Research workbench
Dissection of mannosylglycerate synthase: an archetypal mannosyltransferase
Analyse Dissection of mannosylglycerate synthase: an archetypal mannosyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BO6
- Type
- protein
- Length
- 760 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mannosylglycerate synthase
- EC
- 2.4.1.-
- UniProt
- Q9RFR0
- Ligands
- DGY, MN
- Pockets
- 5 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Mannosylglycerate synthase (EC 2.4.1.-) | protein | 380 | 53% helix, 10% strand | Q9RFR0 |
Ligands and binding sites
- DGY · (2R)-2,3-dihydroxypropanoic acid · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 536 | 0.76 | 0.83 | 49 | DGY, MN |
| 2 | 521 | 0.75 | 0.83 | 55 | DGY, MN |
| 3 | 89 | 0.53 | 0.84 | 22 | empty |
| 4 | 97 | 0.50 | 0.82 | 20 | empty |
| 5 | 111 | 0.39 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1191 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 2BO6 · Dissection of mannosylglycerate synthase: an archetypal mannosyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
- Q9RFR0 · AlphaFold monomer V2.0 prediction for mannosylglycerate synthase (Q9RFR0) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9RFR0
- Elsewhere: RCSB PDB 2BO6 · PDBe 2BO6 · UniProt Q9RFR0
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