Research workbench
Crystal structure of 4-alpha-glucanotransferase from thermococcus litoralis
Analyse Crystal structure of 4-alpha-glucanotransferase from thermococcus litoralis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K1W
- Type
- protein
- Length
- 628 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
- O32462
- Ligands
- GLC, CA, SO4
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-alpha-glucanotransferase (EC 2.4.1.25) | protein | 628 | 32% helix, 29% strand | O32462 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · chains A
- CA · Calcium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1104 | 0.78 | 0.80 | 94 | GLC |
| 2 | 128 | 0.63 | 0.86 | 29 | empty |
| 3 | 63 | 0.35 | 0.77 | 13 | empty |
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
- 1K1W · Crystal structure of 4-alpha-glucanotransferase from thermococcus litoralis · the same entry in another collection · chain A against A, TM-score 1.00
- O32462 · AlphaFold monomer V2.0 prediction for 4-alpha-glucanotransferase (O32462) · 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 O32462
- Elsewhere: RCSB PDB 1K1W · PDBe 1K1W · UniProt O32462
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