MolNFT v1 · #155593 · protein
Ttgala, alpha-galactosidase from thermus thermopilus in apo form
6LCJ: “Ttgala, alpha-galactosidase from thermus thermopilus in apo form”. X-ray diffraction, 20 pockets (best druggability 0.78). MolNFT v1 #155593 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6LCJ
- Type
- protein
- Length
- 2,833 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-galactosidase
- UniProt
- Q53W51
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | Alpha-galactosidase | protein | 479 | 30% helix, 30% strand | Q53W51 |
| B | Alpha-galactosidase | protein | 478 | 30% helix, 29% strand | Q53W51 |
| D | Alpha-galactosidase | protein | 460 | 31% helix, 28% strand | Q53W51 |
| F | Alpha-galactosidase | protein | 458 | 31% helix, 29% strand | Q53W51 |
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 | 639 | 0.78 | 0.84 | 78 | empty |
| 2 | 382 | 0.74 | 0.85 | 45 | empty |
| 3 | 676 | 0.74 | 0.80 | 76 | empty |
| 4 | 914 | 0.74 | 0.78 | 84 | empty |
| 5 | 351 | 0.65 | 0.80 | 52 | empty |
Interfaces
9 interfaces between chains.
- E–F · 707 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 685 Ų buried · 10 hydrogen bonds · protein-protein
- A–F · 597 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 581 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 581 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6LCJ · TtGalA, alpha-galactosidase from Thermus thermopilus in apo form · 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 Q53W51
- Elsewhere: RCSB PDB 6LCJ · PDBe 6LCJ · UniProt Q53W51
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