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The crystal structure of native glycosidic hydrolase
Analyse The crystal structure of native glycosidic hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WVJ
- Type
- protein
- Length
- 439 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-glucanase
- EC
- 3.2.1.73
- UniProt
- A3DBX3
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-glucanase (EC 3.2.1.73) | protein | 219 | 6% helix, 52% strand | A3DBX3 |
| B | Beta-glucanase (EC 3.2.1.73) | protein | 220 | 6% helix, 51% strand | A3DBX3 |
Ligands and binding sites
- B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 265 | 0.65 | 0.82 | 43 | B3P |
| 2 | 270 | 0.65 | 0.81 | 38 | B3P |
| 3 | 289 | 0.59 | 0.78 | 41 | empty |
Interfaces
1 interface between chains.
- A–B · 906 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
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 A3DBX3
- Elsewhere: RCSB PDB 3WVJ · PDBe 3WVJ · UniProt A3DBX3
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