Research workbench
Complex between a udp-glucosyltransferase from polygonum tinctorium capable of glucosylating indoxyl and udp-glucose
Analyse Complex between a udp-glucosyltransferase from polygonum tinctorium capable of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SU6
- Type
- protein
- Length
- 922 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyltransferase
- EC
- 2.4.1.-
- UniProt
- A0A2R2JFJ4
- Ligands
- UPG
- Pockets
- 15 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyltransferase (EC 2.4.1.-) | protein | 467 | 44% helix, 14% strand | A0A2R2JFJ4 |
| B | Glycosyltransferase (EC 2.4.1.-) | protein | 455 | 43% helix, 14% strand | A0A2R2JFJ4 |
Ligands and binding sites
- UPG · Uridine-5'-diphosphate-glucose · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 489 | 0.72 | 0.81 | 49 | UPG |
| 2 | 480 | 0.70 | 0.80 | 49 | UPG |
| 3 | 415 | 0.63 | 0.77 | 42 | empty |
| 4 | 244 | 0.54 | 0.77 | 30 | empty |
| 5 | 114 | 0.45 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 849 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6SU6 · Complex between a UDP-glucosyltransferase from Polygonum tinctorium capable of… · 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 A0A2R2JFJ4
- Elsewhere: RCSB PDB 6SU6 · PDBe 6SU6 · UniProt A0A2R2JFJ4
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