Research workbench
Crystal structure of thermus thermophilus A4 beta-galactosidase
Analyse Crystal structure of thermus thermophilus A4 beta-galactosidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KWG
- Type
- protein
- Length
- 644 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-galactosidase
- EC
- 3.2.1.23
- UniProt
- O69315
- Ligands
- ZN, CL
- Pockets
- 8 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-galactosidase (EC 3.2.1.23) | protein | 644 | 35% helix, 19% strand | O69315 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- CL · Chloride ion · ion · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 861 | 0.71 | 0.76 | 89 | ACT, MPD |
| 2 | 198 | 0.48 | 0.75 | 27 | empty |
| 3 | 120 | 0.45 | 0.78 | 19 | empty |
| 4 | 117 | 0.42 | 0.77 | 30 | empty |
| 5 | 139 | 0.41 | 0.75 | 29 | empty |
Compared structures
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 O69315
- Elsewhere: RCSB PDB 1KWG · PDBe 1KWG · UniProt O69315
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