Research workbench
The three-dimensional structure of 6-phospho-beta galactosidase from lactococcus lactis
Analyse The three-dimensional structure of 6-phospho-beta galactosidase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PBG
- Type
- protein
- Length
- 910 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 6-phospho-beta-D-galactosidase
- EC
- 3.2.1.85
- UniProt
- P11546
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 6-phospho-beta-D-galactosidase (EC 3.2.1.85) | protein | 454 | 43% helix, 18% strand | P11546 |
| B | 6-phospho-beta-D-galactosidase (EC 3.2.1.85) | protein | 456 | 43% helix, 19% strand | P11546 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 810 | 0.76 | 0.80 | 55 | SO4 |
| 2 | 560 | 0.74 | 0.81 | 46 | SO4 |
| 3 | 113 | 0.37 | 0.74 | 16 | empty |
| 4 | 111 | 0.37 | 0.74 | 16 | empty |
Compared structures
- 1PBG · The three-dimensional structure of 6-phospho-beta galactosidase from lactococcus lactis · the same entry in another collection · chain A against A, TM-score 1.00
- P11546 · AlphaFold monomer V2.0 prediction for 6-phospho-beta-galactosidase (P11546) · 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 P11546
- Elsewhere: RCSB PDB 1PBG · PDBe 1PBG · UniProt P11546
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