Research workbench
Crystal structure of glucose dehydrogenase of caenorhabditis elegans in the apo-form
Analyse Crystal structure of glucose dehydrogenase of caenorhabditis elegans in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SPX
- Type
- protein
- Length
- 237 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Short-chain reductase family member (5L265)
- EC
- 1.1.1.47
- UniProt
- Q18946
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Short-chain reductase family member (5L265) (EC 1.1.1.47) | protein | 237 | 53% helix, 16% strand | Q18946 |
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 | 242 | 0.51 | 0.75 | 44 | empty |
Compared structures
- 1SPX · Crystal Structure of Glucose Dehydrogenase of Caenorhabditis Elegans in the Apo-Form · 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 Q18946
- Elsewhere: RCSB PDB 1SPX · PDBe 1SPX · UniProt Q18946
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