Research workbench
Disproportionating enzyme 1 from arabidopsis - cycloamylose soak
Analyse Disproportionating enzyme 1 from arabidopsis - cycloamylose soak in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CQ1
- Type
- protein
- Length
- 1,025 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9LV91
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 514 | — | Q9LV91 |
| B | — | protein | 511 | — | Q9LV91 |
Compared structures
- Q9LV91 · AlphaFold monomer V2.0 prediction for 4-alpha-glucanotransferase DPE1… · a predicted model of the same protein · chain B 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 Q9LV91
- Elsewhere: RCSB PDB 5CQ1 · PDBe 5CQ1 · UniProt Q9LV91
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