Research workbench
The complex structure of HYPBA1 with L-arabinose
Analyse The complex structure of HYPBA1 with L-arabinose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WRG
- Type
- protein
- Length
- 658 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-reducing end beta-L-arabinofuranosidase
- EC
- 3.2.1.185
- UniProt
- E8MGH8
- Ligands
- FUB, ZN
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-reducing end beta-L-arabinofuranosidase (EC 3.2.1.185) | protein | 658 | 39% helix, 17% strand | E8MGH8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.72 | 0.97 | 29 | FUB |
| 2 | 334 | 0.66 | 0.81 | 31 | empty |
| 3 | 326 | 0.60 | 0.77 | 35 | empty |
| 4 | 115 | 0.45 | 0.78 | 16 | empty |
| 5 | 75 | 0.35 | 0.75 | 16 | empty |
Compared structures
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 E8MGH8
- Elsewhere: RCSB PDB 3WRG · PDBe 3WRG · UniProt E8MGH8
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