Research workbench
Structure of beta-galactosidase from thermotoga maritima.
Analyse Structure of beta-galactosidase from thermotoga maritima. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SD0
- Type
- protein
- Length
- 4,332 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-galactosidase
- EC
- 3.2.1.23
- UniProt
- Q56307
- Ligands
- MG
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Beta-galactosidase (EC 3.2.1.23) | protein | 1083 | 13% helix, 43% strand | Q56307 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1152 | 0.86 | 0.87 | 122 | empty |
| 2 | 353 | 0.75 | 0.86 | 50 | empty |
| 3 | 324 | 0.74 | 0.86 | 50 | empty |
| 4 | 335 | 0.73 | 0.85 | 50 | empty |
| 5 | 70 | 0.73 | 0.98 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 887 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 181 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 165 Ų buried · 4 hydrogen bonds · protein-protein
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 Q56307
- Elsewhere: RCSB PDB 6SD0 · PDBe 6SD0 · UniProt Q56307
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