Research workbench
D341A D367A calcium binding mutant of bacteroides uniformis beta- glucuronidase 2
Analyse D341A D367A calcium binding mutant of bacteroides uniformis beta- glucuronidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6D8G
- Type
- protein
- Length
- 1,663 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyl hydrolases family 2, sugar binding domain protein
- UniProt
- A0A078SUX9
- Ligands
- NA
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyl hydrolases family 2, sugar binding domain protein | protein | 832 | 15% helix, 42% strand | A0A078SUX9 |
| B | Glycosyl hydrolases family 2, sugar binding domain protein | protein | 831 | 15% helix, 43% strand | A0A078SUX9 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 614 | 0.87 | 0.92 | 65 | empty |
| 2 | 964 | 0.86 | 0.87 | 103 | empty |
| 3 | 814 | 0.85 | 0.88 | 105 | empty |
| 4 | 181 | 0.70 | 0.88 | 25 | empty |
| 5 | 258 | 0.70 | 0.85 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 3511 Ų buried · 62 hydrogen bonds · protein-protein
Compared structures
- 6D8G · D341A D367A calcium binding mutant of Bacteroides uniformis beta-glucuronidase 2 · 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 A0A078SUX9
- Elsewhere: RCSB PDB 6D8G · PDBe 6D8G · UniProt A0A078SUX9
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