Research workbench
Crystal structure of barley exohydrolasei W434A mutant in complex with glucose.
Analyse Crystal structure of barley exohydrolasei W434A mutant in complex with glucose. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KUF
- Type
- protein
- Length
- 606 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-D-glucan glucohydrolase isoenzyme EXO1
- UniProt
- A0A287SCR5
- Ligands
- NAG, BGC, SO4
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-D-glucan glucohydrolase isoenzyme EXO1 | protein | 606 | 38% helix, 12% strand | A0A287SCR5 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- BGC · beta-D-glucopyranose · sugar · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 5 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.49 | 0.81 | 21 | BGC, GOL |
| 2 | 67 | 0.32 | 0.75 | 18 | empty |
Modifications
Observed in the structure: 3 glycan, 2 disulfide (N-glycosylation, disulfide).
Compared structures
- 6KUF · Crystal structure of barley exohydrolaseI W434A mutant in complex with glucose. · 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 A0A287SCR5
- Elsewhere: RCSB PDB 6KUF · PDBe 6KUF · UniProt A0A287SCR5
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