Research workbench
Alcohol dehydrogenase from entamoeba histolotica in complex with cacodylate
Analyse Alcohol dehydrogenase from entamoeba histolotica in complex with cacodylate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y9A
- Type
- protein
- Length
- 720 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P35630
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 360 | — | P35630 |
Compared structures
- 1Y9A · Alcohol Dehydrogenase from Entamoeba histolotica in complex with cacodylate · the same entry in another collection · chain A against A, TM-score 1.00
- P35630 · AlphaFold monomer V2.0 prediction for NADP-dependent isopropanol dehydrogenase (P35630) · a predicted model of the same protein · 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 P35630
- Elsewhere: RCSB PDB 1Y9A · PDBe 1Y9A · UniProt P35630
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.