MolNFT v1 · #30258 · protein
Crystal structure of alpha-galactosidase (ec 3.2.1.22) (melibiase) (TM1192) from thermotoga maritima at 2.34 a resolution
1ZY9: “Crystal structure of alpha-galactosidase (ec 3.2.1.22) (melibiase) (TM1192) from thermotoga maritima at 2.34…”. X-ray diffraction, 3 pockets (best druggability 0.70). MolNFT v1 #30258 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1ZY9
- Type
- protein
- Length
- 526 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-galactosidase
- EC
- 3.2.1.22
- UniProt
- O33835
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-galactosidase (EC 3.2.1.22) | protein | 526 | 28% helix, 34% strand | O33835 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 445 | 0.70 | 0.81 | 47 | EDO, GOL |
| 2 | 64 | 0.33 | 0.76 | 14 | empty |
| 3 | 50 | 0.30 | 0.76 | 13 | empty |
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 1ZY9 · Crystal structure of Alpha-galactosidase (EC 3.2.1.22) (Melibiase) (tm1192) from… · 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 O33835
- Elsewhere: RCSB PDB 1ZY9 · PDBe 1ZY9 · UniProt O33835
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