Research workbench
Crystal structure of a family 51 (GH51) alpha-L-arabinofuranosidase from geobacillus stearothermophilus T6
Analyse Crystal structure of a family 51 (GH51) alpha-L-arabinofuranosidase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PZ3
- Type
- protein
- Length
- 994 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-L-arabinofuranosidase
- EC
- 3.2.1.55
- UniProt
- Q9XBQ3
- Pockets
- 6 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alpha-L-arabinofuranosidase (EC 3.2.1.55) | protein | 497 | 29% helix, 27% strand | Q9XBQ3 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 860 | 0.68 | 0.75 | 73 | empty |
| 2 | 261 | 0.52 | 0.75 | 47 | GOL |
| 3 | 216 | 0.51 | 0.76 | 34 | GOL |
| 4 | 75 | 0.46 | 0.82 | 16 | empty |
| 5 | 53 | 0.34 | 0.78 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 995 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1PZ3 · Crystal structure of a family 51 (GH51) alpha-L-arabinofuranosidase from Geobacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9XBQ3 · AlphaFold monomer V2.0 prediction for intracellular exo… · a predicted model of the same protein · 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 Q9XBQ3
- Elsewhere: RCSB PDB 1PZ3 · PDBe 1PZ3 · UniProt Q9XBQ3
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