MolNFT v1 · #24275 · protein
GLCNAC[ALPHA]1-4GAL releasing endo-[beta]-galactosidase from clostridium perfringens
1UPS · Glcnac-alpha-1,4-gal-releasing endo-beta-galactosidase: “GLCNAC[ALPHA]1-4GAL releasing endo-[beta]-galactosidase from clostridium perfringens”. X-ray diffraction, 1 ligand (CA), 7 pockets (best druggability 0.70). MolNFT v1 #24275…
- PDB
- 1UPS
- Type
- protein
- Length
- 799 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glcnac-alpha-1,4-gal-releasing endo-beta-galactosidase
- UniProt
- Q934G8
- Ligands
- CA
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glcnac-alpha-1,4-gal-releasing endo-beta-galactosidase | protein | 402 | 5% helix, 42% strand | Q934G8 |
| B | Glcnac-alpha-1,4-gal-releasing endo-beta-galactosidase | protein | 397 | 5% helix, 41% strand | Q934G8 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 517 | 0.70 | 0.79 | 43 | empty |
| 2 | 440 | 0.68 | 0.79 | 38 | empty |
| 3 | 370 | 0.55 | 0.74 | 47 | empty |
| 4 | 230 | 0.49 | 0.74 | 32 | empty |
| 5 | 153 | 0.43 | 0.75 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 745 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1UPS · GlcNAc[alpha]1-4Gal releasing endo-[beta]-galactosidase from Clostridium perfringens · 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 Q934G8
- Elsewhere: RCSB PDB 1UPS · PDBe 1UPS · UniProt Q934G8
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