Research workbench
Crystal structure of TETUR04G02350
Analyse Crystal structure of TETUR04G02350 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LVY
- Type
- protein
- Length
- 431 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-glycosyltransferase 203A2
- UniProt
- T1K1R5
- Ligands
- UDP, BGC
- Pockets
- 4 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-glycosyltransferase 203A2 | protein | 431 | 46% helix, 14% strand | T1K1R5 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · chains A
- BGC · beta-D-glucopyranose · sugar · 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 | 818 | 0.85 | 0.87 | 83 | UDP, BGC |
| 2 | 109 | 0.49 | 0.81 | 25 | empty |
| 3 | 59 | 0.36 | 0.79 | 16 | empty |
| 4 | 65 | 0.33 | 0.77 | 12 | empty |
Compared structures
- 7LVY · Crystal Structure of Tetur04g02350 · 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 T1K1R5
- Elsewhere: RCSB PDB 7LVY · PDBe 7LVY · UniProt T1K1R5
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