Research workbench
Crystal structure of fagopyrum esculentum M UGT708C1 complexed with udp
Analyse Crystal structure of fagopyrum esculentum M UGT708C1 complexed with udp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LLW
- Type
- protein
- Length
- 857 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-glycosyltransferase 708C1
- EC
- 2.4.1.-
- UniProt
- A0A0A1HA03
- Ligands
- UDP
- Pockets
- 11 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-glycosyltransferase 708C1 (EC 2.4.1.-) | protein | 433 | 48% helix, 15% strand | A0A0A1HA03 |
| B | Udp-glycosyltransferase 708C1 (EC 2.4.1.-) | protein | 424 | 48% helix, 15% strand | A0A0A1HA03 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 888 | 0.81 | 0.83 | 88 | UDP |
| 2 | 896 | 0.81 | 0.83 | 75 | UDP |
| 3 | 565 | 0.70 | 0.79 | 49 | empty |
| 4 | 54 | 0.45 | 0.84 | 14 | empty |
| 5 | 60 | 0.43 | 0.82 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 374 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6LLW · Crystal Structure of Fagopyrum esculentum M UGT708C1 complexed with UDP · 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 A0A0A1HA03
- Elsewhere: RCSB PDB 6LLW · PDBe 6LLW · UniProt A0A0A1HA03
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