Research workbench
Structure of the family GH92 alpha-mannosidase BT3130 from bacteroides thetaiotaomicron
Analyse Structure of the family GH92 alpha-mannosidase BT3130 from bacteroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F8Z
- Type
- protein
- Length
- 2,118 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1,2-mannosidase, putative
- UniProt
- A0A174L250
- Ligands
- CA
- Pockets
- 20 · best druggability 0.66
Structure
x-ray diffraction · 3 distinct chains · 30% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1,2-mannosidase, putative | protein | 715 | 29% helix, 25% strand | A0A174L250 |
| B | Alpha-1,2-mannosidase, putative | protein | 703 | 30% helix, 24% strand | A0A174L250 |
| C | Alpha-1,2-mannosidase, putative | protein | 700 | 31% helix, 23% strand | A0A174L250 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 728 | 0.66 | 0.75 | 92 | empty |
| 2 | 250 | 0.55 | 0.78 | 46 | empty |
| 3 | 289 | 0.55 | 0.76 | 47 | CA |
| 4 | 268 | 0.54 | 0.76 | 48 | CA |
| 5 | 76 | 0.46 | 0.82 | 16 | empty |
Interfaces
2 interfaces between chains.
- B–C · 1529 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 677 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6F8Z · Structure of the family GH92 alpha-mannosidase BT3130 from Bacteroides thetaiotaomicron · 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 A0A174L250
- Elsewhere: RCSB PDB 6F8Z · PDBe 6F8Z · UniProt A0A174L250
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