MolNFT v1 · #74114 · protein
Crystal structure of an exo-alpha-1,6-mannosidase (BACOVA_03626) from bacteroides ovatus at 1.70 a resolution
3ON6 · Uncharacterized protein: “Crystal structure of an exo-alpha-1,6-mannosidase (BACOVA_03626) from bacteroides ovatus at 1.70 a resolution”. X-ray diffraction, 1 ligand (CL), 9 pockets (best druggability 0.78). MolNFT v1 #74114 on…
- PDB
- 3ON6
- Type
- protein
- Length
- 886 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- A7M0J6
- Ligands
- CL
- Pockets
- 9 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Uncharacterized protein | protein | 443 | 48% helix, 12% strand | A7M0J6 |
Ligands and binding sites
- CL · Chloride ion · ion · 4 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 9 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 120 | 0.78 | 0.96 | 35 | EDO |
| 2 | 153 | 0.51 | 0.79 | 25 | EDO |
| 3 | 152 | 0.50 | 0.79 | 25 | EDO |
| 4 | 147 | 0.48 | 0.78 | 21 | EDO |
| 5 | 122 | 0.48 | 0.79 | 19 | EDO |
Interfaces
1 interface between chains.
- A–B · 1620 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 30 modified (engineered).
Compared structures
- 3ON6 · Crystal structure of an exo-alpha-1,6-mannosidase (bacova_03626) from bacteroides ovatus… · 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 A7M0J6
- Elsewhere: RCSB PDB 3ON6 · PDBe 3ON6 · UniProt A7M0J6
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