Research workbench
Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility
Analyse Evidence that GH115 alpha-glucuronidase activity is dependent on conformational… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C90
- Type
- protein
- Length
- 1,633 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-glucuronidase GH115
- UniProt
- A7M022
- Ligands
- NA
- Pockets
- 15 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-glucuronidase GH115 | protein | 822 | 35% helix, 19% strand | A7M022 |
| B | Alpha-glucuronidase GH115 | protein | 811 | 36% helix, 19% strand | A7M022 |
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
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.78 | 0.86 | 44 | empty |
| 2 | 398 | 0.76 | 0.86 | 49 | empty |
| 3 | 605 | 0.71 | 0.79 | 68 | empty |
| 4 | 455 | 0.68 | 0.79 | 41 | empty |
| 5 | 375 | 0.63 | 0.78 | 40 | empty |
Interfaces
1 interface between chains.
- A–B · 4209 Ų buried · 59 hydrogen bonds · protein-protein
Compared structures
- 4C90 · Evidence that GH115 alpha-glucuronidase activity is dependent on conformational… · 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 A7M022
- Elsewhere: RCSB PDB 4C90 · PDBe 4C90 · UniProt A7M022
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