MolNFT v1 · #72469 · protein
F229A/E292S double mutant of exo-beta-1,3-glucanase from candida albicans in complex with laminaritriose at 1.7 a
3N9K · Glucan 1,3-beta-glucosidase: “F229A/E292S double mutant of exo-beta-1,3-glucanase from candida albicans in complex with laminaritriose at…”. X-ray diffraction, 2 ligands (BGC, CA), 2 pockets (best druggability 0.65). MolNFT v1…
- PDB
- 3N9K
- Type
- protein
- Length
- 394 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucan 1,3-beta-glucosidase
- EC
- 3.2.1.58
- UniProt
- P29717
- Ligands
- BGC, CA
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucan 1,3-beta-glucosidase (EC 3.2.1.58) | protein | 394 | 39% helix, 12% strand | P29717 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.65 | 0.80 | 42 | BGC |
| 2 | 78 | 0.36 | 0.76 | 21 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3N9K · F229A/E292S Double Mutant of Exo-beta-1,3-glucanase from Candida albicans in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P29717 · AlphaFold monomer V2.0 prediction for glucan 1,3-beta-glucosidase (P29717) · a predicted model of the same protein · 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 P29717
- Elsewhere: RCSB PDB 3N9K · PDBe 3N9K · UniProt P29717
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