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Crystal structure of ugt transferase mutant in complex with upg
Analyse Crystal structure of ugt transferase mutant in complex with upg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L8Z
- Type
- protein
- Length
- 444 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyltransferase
- EC
- 2.4.1.-
- UniProt
- K7NBW3
- Ligands
- UPG
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyltransferase (EC 2.4.1.-) | protein | 444 | 46% helix, 14% strand | K7NBW3 |
Ligands and binding sites
- UPG · Uridine-5'-diphosphate-glucose · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1077 | 0.73 | 0.76 | 77 | UPG |
| 2 | 90 | 0.57 | 0.86 | 19 | empty |
| 3 | 209 | 0.52 | 0.77 | 25 | empty |
| 4 | 71 | 0.38 | 0.78 | 14 | empty |
| 5 | 60 | 0.30 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 K7NBW3
- Elsewhere: RCSB PDB 6L8Z · PDBe 6L8Z · UniProt K7NBW3
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