Research workbench
Structure of arabidopsis dirigent protein ATDIR6
Analyse Structure of arabidopsis dirigent protein ATDIR6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LAL
- Type
- protein
- Length
- 308 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dirigent protein 6
- UniProt
- Q9SUQ8
- Ligands
- GLY, NAG, MAN, BMA, XYP, FUC
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dirigent protein 6 | protein | 153 | 0% helix, 57% strand | Q9SUQ8 |
| B | Dirigent protein 6 | protein | 155 | 0% helix, 57% strand | Q9SUQ8 |
Ligands and binding sites
- GLY · Glycine · ligand · 5 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
- MAN · alpha-D-mannopyranose · sugar · 6 copies · chains B
- BMA · beta-D-mannopyranose · sugar · 3 copies
- XYP · beta-D-xylopyranose · sugar · 3 copies · chains A, B
- FUC · alpha-L-fucopyranose · sugar · 3 copies · chains B, A
- EDO · 1,2-ethanediol · additive · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.59 | 0.84 | 24 | GLY |
Interfaces
1 interface between chains.
- A–B · 460 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 glycan, 2 disulfide (N-glycosylation, 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 Q9SUQ8
- Elsewhere: RCSB PDB 5LAL · PDBe 5LAL · UniProt Q9SUQ8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.