Research workbench
Crystal structure analysis of plant exohydrolase
Analyse Crystal structure analysis of plant exohydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WLH
- Type
- protein
- Length
- 602 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-D-glucan exohydrolase isoenzyme exoi
- UniProt
- Q9XEI3
- Ligands
- NAG, BMA, FUL, BGC, MAN, XYP, SO4
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-D-glucan exohydrolase isoenzyme exoi | protein | 602 | 38% helix, 13% strand | Q9XEI3 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 3 copies
- FUL · beta-L-fucopyranose · sugar · 2 copies · chains A
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · chains A
- XYP · beta-D-xylopyranose · sugar · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 3 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.50 | 0.83 | 20 | BGC |
| 2 | 59 | 0.31 | 0.76 | 19 | empty |
Modifications
Observed in the structure: 3 glycan, 2 disulfide (N-glycosylation, disulfide).
Compared structures
- 3WLH · Crystal Structure Analysis of Plant Exohydrolase · 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 Q9XEI3
- Elsewhere: RCSB PDB 3WLH · PDBe 3WLH · UniProt Q9XEI3
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