MolNFT v1 · #26840 · protein
Structure determination and refinement at 1.8 a resolution of disproportionating enzyme from potato
1X1N · 4-alpha-glucanotransferase: “Structure determination and refinement at 1.8 a resolution of disproportionating enzyme from potato”. X-ray diffraction, 1 ligand (CA), 4 pockets (best druggability 0.77). MolNFT v1 #26840 on GenesisL1…
- PDB
- 1X1N
- Type
- protein
- Length
- 523 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-alpha-glucanotransferase
- EC
- 2.4.1.25
- UniProt
- Q06801
- Ligands
- CA
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-alpha-glucanotransferase (EC 2.4.1.25) | protein | 523 | 45% helix, 12% strand | Q06801 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1110 | 0.77 | 0.79 | 104 | GOL |
| 2 | 195 | 0.52 | 0.78 | 27 | empty |
| 3 | 83 | 0.51 | 0.84 | 18 | GOL |
| 4 | 97 | 0.34 | 0.74 | 19 | empty |
Compared structures
- 1X1N · Structure determination and refinement at 1.8 A resolution of Disproportionating Enzyme… · the same entry in another collection · chain A against A, TM-score 1.00
- Q06801 · AlphaFold monomer V2.0 prediction for 4-alpha-glucanotransferase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q06801
- Elsewhere: RCSB PDB 1X1N · PDBe 1X1N · UniProt Q06801
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