Research workbench
E. COLI (lacz) beta-galactosidase (N460T)
Analyse E. COLI (lacz) beta-galactosidase (N460T) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VDA
- Type
- protein
- Length
- 4,060 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-galactosidase
- EC
- 3.2.1.23
- UniProt
- P00722
- Ligands
- NA, MG
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Beta-galactosidase (EC 3.2.1.23) | protein | 1015 | 14% helix, 40% strand | P00722 |
Ligands and binding sites
- NA · Sodium ion · metal · 10 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 8 copies · chains A, B, C, D
- DMS · Dimethyl sulfoxide · additive · 32 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 892 | 0.80 | 0.83 | 99 | empty |
| 2 | 775 | 0.79 | 0.83 | 105 | DMS |
| 3 | 607 | 0.76 | 0.83 | 69 | empty |
| 4 | 1175 | 0.75 | 0.78 | 103 | DMS |
| 5 | 1147 | 0.75 | 0.78 | 100 | empty |
Interfaces
6 interfaces between chains.
- A–D · 2540 Ų buried · 32 hydrogen bonds · protein-protein
- B–C · 2499 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 2092 Ų buried · 23 hydrogen bonds · protein-protein
- C–D · 2048 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 143 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 P00722
- Elsewhere: RCSB PDB 3VDA · PDBe 3VDA · UniProt P00722
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