Research workbench
Crystal structure of OS79 from O. sativa in complex with udp.
Analyse Crystal structure of OS79 from O. sativa in complex with udp. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TME
- Type
- protein
- Length
- 435 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyltransferase, OS79
- EC
- 2.4.1.-
- UniProt
- Q7XT97
- Ligands
- UDP
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyltransferase, OS79 (EC 2.4.1.-) | protein | 435 | 47% helix, 13% strand | Q7XT97 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 817 | 0.77 | 0.81 | 58 | UDP |
| 2 | 165 | 0.46 | 0.75 | 31 | empty |
| 3 | 72 | 0.44 | 0.81 | 15 | empty |
| 4 | 101 | 0.41 | 0.77 | 17 | empty |
| 5 | 51 | 0.38 | 0.81 | 13 | 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 Q7XT97
- Elsewhere: RCSB PDB 5TME · PDBe 5TME · UniProt Q7XT97
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