Research workbench
Crystal structure of fructan 1-exohydrolase iia from cichorium intybus in complex with sucrose
Analyse Crystal structure of fructan 1-exohydrolase iia from cichorium intybus in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ADD
- Type
- protein
- Length
- 537 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructan 1-exohydrolase iia
- EC
- 3.2.1.153
- UniProt
- Q93X60
- Ligands
- NAG, MAN, GLC, FRU
- Pockets
- 4 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructan 1-exohydrolase iia (EC 3.2.1.153) | protein | 537 | 6% helix, 47% strand | Q93X60 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- MAN · alpha-D-mannopyranose · sugar
- GLC · alpha-D-glucopyranose · sugar · chains A
- FRU · beta-D-fructofuranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 375 | 0.61 | 0.77 | 42 | empty |
| 2 | 143 | 0.55 | 0.81 | 25 | empty |
| 3 | 94 | 0.39 | 0.76 | 14 | GLC, FRU |
| 4 | 51 | 0.27 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 2 glycan, 1 disulfide (N-glycosylation, disulfide).
Compared structures
- 2ADD · Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with… · 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 Q93X60
- Elsewhere: RCSB PDB 2ADD · PDBe 2ADD · UniProt Q93X60
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