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Cold-adapted beta-D-galactosidase from arthrobacter sp. 32CB mutant E441Q in complex with lactose bound in shallow mode
Analyse Cold-adapted beta-D-galactosidase from arthrobacter sp. 32CB mutant E441Q in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SE9
- Type
- protein
- Length
- 989 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-galactosidase
- EC
- 3.2.1.23
- UniProt
- A0A023UGN9
- Ligands
- GAL, FRU, BGC, NA
- Pockets
- 16 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-galactosidase (EC 3.2.1.23) | protein | 989 | 16% helix, 37% strand | A0A023UGN9 |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A
- FRU · beta-D-fructofuranose · sugar · 2 copies · chains A
- BGC · beta-D-glucopyranose · sugar · chains A
- NA · Sodium ion · metal · 2 copies · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- MLI · Malonate ion · additive · chains A
- FMT · Formic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.64 | 0.84 | 27 | empty |
| 2 | 205 | 0.55 | 0.79 | 32 | empty |
| 3 | 76 | 0.52 | 0.85 | 16 | empty |
| 4 | 78 | 0.51 | 0.85 | 15 | empty |
| 5 | 179 | 0.48 | 0.76 | 28 | empty |
Compared structures
- 6SE9 · Cold-adapted beta-D-galactosidase from Arthrobacter sp. 32cB mutant E441Q in complex with… · the same entry in another collection · chain A 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 A0A023UGN9
- Elsewhere: RCSB PDB 6SE9 · PDBe 6SE9 · UniProt A0A023UGN9
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