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A glycosyltransferase with udp and the substrate
Analyse A glycosyltransferase with udp and the substrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6INH
- Type
- protein
- Length
- 450 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-glycosyltransferase 76G1
- EC
- 2.4.1.-
- UniProt
- Q6VAB4
- Ligands
- AQ9, UDP
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-glycosyltransferase 76G1 (EC 2.4.1.-) | protein | 450 | 45% helix, 16% strand | Q6VAB4 |
Ligands and binding sites
- AQ9 · 1-O-[(8alpha,9beta,10alpha,13alpha)-13-(beta-D-glucopyranosyloxy)-18-oxokaur-16-en-18-yl]-beta-D-glucopyranose · ligand · 2 copies · chains A
- UDP · Uridine-5'-diphosphate · ligand · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 745 | 0.82 | 0.85 | 63 | UDP, AQ9, GOL |
| 2 | 99 | 0.46 | 0.80 | 15 | empty |
| 3 | 86 | 0.32 | 0.73 | 16 | empty |
| 4 | 57 | 0.28 | 0.74 | 17 | empty |
Compared structures
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 Q6VAB4
- Elsewhere: RCSB PDB 6INH · PDBe 6INH · UniProt Q6VAB4
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