Research workbench
Crystal structure of the sorghum bicolor dhurrinase 1
Analyse Crystal structure of the sorghum bicolor dhurrinase 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V03
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dhurrinase
- EC
- 3.2.1.21
- UniProt
- Q41290
- Ligands
- CCN, IPH, BGC
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dhurrinase (EC 3.2.1.21) | protein | 487 | 44% helix, 17% strand | Q41290 |
Ligands and binding sites
- CCN · Acetonitrile · ligand · chains A
- IPH · Phenol · ligand · chains A
- BGC · beta-D-glucopyranose · sugar · chains A
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 | 466 | 0.69 | 0.80 | 48 | BGC, CCN, IPH |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1V03 · Crystal structure of the Sorghum bicolor dhurrinase 1 · 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 Q41290
- Elsewhere: RCSB PDB 1V03 · PDBe 1V03 · UniProt Q41290
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.