Research workbench
Crystal structure of arabidopsis thaliana UGT89C1
Analyse Crystal structure of arabidopsis thaliana UGT89C1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IJ7
- Type
- protein
- Length
- 807 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rhamnosyltransferase protein
- EC
- 2.4.1.-
- UniProt
- Q9LNE6
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rhamnosyltransferase protein (EC 2.4.1.-) | protein | 402 | 49% helix, 15% strand | Q9LNE6 |
| B | Rhamnosyltransferase protein (EC 2.4.1.-) | protein | 405 | 48% helix, 16% strand | Q9LNE6 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains A, B
- GOL · Glycerol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1027 | 0.76 | 0.78 | 72 | GOL |
| 2 | 911 | 0.76 | 0.79 | 71 | GOL |
| 3 | 136 | 0.42 | 0.75 | 19 | EDO |
| 4 | 121 | 0.39 | 0.74 | 20 | EDO |
| 5 | 93 | 0.38 | 0.76 | 16 | EDO |
Interfaces
1 interface between chains.
- A–B · 388 Ų buried · 2 hydrogen bonds · protein-protein
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 Q9LNE6
- Elsewhere: RCSB PDB 6IJ7 · PDBe 6IJ7 · UniProt Q9LNE6
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