MolNFT v1 · #24478 · protein
Crystal structure of mutated beta-glycosidase from sulfolobus solfataricus, working at moderate temperature
1UWI · Beta-galactosidase: “Crystal structure of mutated beta-glycosidase from sulfolobus solfataricus, working at moderate temperature”. X-ray diffraction, 14 pockets (best druggability 0.77). MolNFT v1 #24478 on GenesisL1: 3D structure…
- PDB
- 1UWI
- Type
- protein
- Length
- 1,956 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-galactosidase
- EC
- 3.2.1.23
- UniProt
- P22498
- Pockets
- 14 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Beta-galactosidase (EC 3.2.1.23) | protein | 489 | 42% helix, 19% strand | P22498 |
Pockets
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.77 | 0.97 | 22 | empty |
| 2 | 82 | 0.75 | 0.97 | 24 | empty |
| 3 | 995 | 0.73 | 0.76 | 81 | empty |
| 4 | 1029 | 0.73 | 0.76 | 84 | empty |
| 5 | 996 | 0.73 | 0.76 | 83 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1331 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 1326 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 952 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 940 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 73 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1UWI · Crystal structure of mutated beta-glycosidase from sulfolobus solfataricus, working at… · the same entry in another collection · chain D against D, TM-score 1.00
- P22498 · AlphaFold monomer V2.0 prediction for beta-galactosidase (P22498) · a predicted model of the same protein · chain B 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 P22498
- Elsewhere: RCSB PDB 1UWI · PDBe 1UWI · UniProt P22498
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