Research workbench
Crystal structure of GH125 1,6-alpha-mannosidase mutant from clostridium perfringens in complex with 1,6-alpha-mannobiose
Analyse Crystal structure of GH125 1,6-alpha-mannosidase mutant from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5M7I
- Type
- protein
- Length
- 425 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exo-alpha-1,6-mannosidase
- UniProt
- Q8XNB2
- Ligands
- BMA, MAN
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exo-alpha-1,6-mannosidase | protein | 425 | 49% helix, 12% strand | Q8XNB2 |
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 | 122 | 0.55 | 0.83 | 24 | BMA, MAN |
| 2 | 140 | 0.46 | 0.77 | 22 | empty |
| 3 | 52 | 0.29 | 0.75 | 12 | empty |
Compared structures
- 5M7I · Crystal structure of GH125 1,6-alpha-mannosidase mutant from Clostridium perfringens in… · 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 Q8XNB2
- Elsewhere: RCSB PDB 5M7I · PDBe 5M7I · UniProt Q8XNB2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.