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Crystal structure of a GH128 (subgroup III) curdlan-specific exo-beta- 1,3-glucanase from blastomyces gilchristii (BGGH128_III) in complex with glucose
Analyse Crystal structure of a GH128 (subgroup III) curdlan-specific exo-beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UAZ
- Type
- protein
- Length
- 461 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GLYCO_HYDRO_CC domain-containing protein
- UniProt
- A0A179UGT5
- Ligands
- BGC
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GLYCO_HYDRO_CC domain-containing protein | protein | 229 | 41% helix, 22% strand | A0A179UGT5 |
| B | GLYCO_HYDRO_CC domain-containing protein | protein | 232 | 41% helix, 21% strand | A0A179UGT5 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 2 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 581 | 0.69 | 0.78 | 69 | empty |
| 2 | 70 | 0.38 | 0.78 | 19 | empty |
| 3 | 66 | 0.37 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 376 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6UAZ · Crystal structure of a GH128 (subgroup III) curdlan-specific exo-beta-1,3-glucanase from… · 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 A0A179UGT5
- Elsewhere: RCSB PDB 6UAZ · PDBe 6UAZ · UniProt A0A179UGT5
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