Research workbench
X-ray crystal structure of an sco glgei-V279S/1,2,2-trifluromaltose complex
Analyse X-ray crystal structure of an sco glgei-V279S/1,2,2-trifluromaltose complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U2Z
- Type
- protein
- Length
- 1,298 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1,4-GLUCAN:MALTOSE-1-phosphate maltosyltransferase 1
- EC
- 2.4.99.16
- UniProt
- Q9L1K2
- Ligands
- TW7, GLC
- Pockets
- 12 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alpha-1,4-GLUCAN:MALTOSE-1-phosphate maltosyltransferase 1 (EC 2.4.99.16) | protein | 649 | 34% helix, 25% strand | Q9L1K2 |
Ligands and binding sites
- TW7 · 2-deoxy-2,2-difluoro-alpha-D-arabino-hexopyranosyl fluoride · ligand · 2 copies · chains A, B
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1022 | 0.80 | 0.81 | 82 | TW7, GLC |
| 2 | 769 | 0.76 | 0.80 | 51 | empty |
| 3 | 1179 | 0.73 | 0.76 | 114 | empty |
| 4 | 313 | 0.69 | 0.83 | 38 | TW7, GLC |
| 5 | 115 | 0.52 | 0.82 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2304 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 4U2Z · X-ray crystal structure of an Sco GlgEI-V279S/1,2,2-trifluromaltose complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9L1K2 · AlphaFold monomer V2.0 prediction for alpha-1,4-GLUCAN:MALTOSE-1-phosphate… · 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 Q9L1K2
- Elsewhere: RCSB PDB 4U2Z · PDBe 4U2Z · UniProt Q9L1K2
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