MolNFT v1 · #141377 · protein
Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from geobacillus thermoleovorans it-08 in complex with D-xylose
5Z5H · Beta-xylosidase: “Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from geobacillus…”. X-ray diffraction, 2 ligands (XYS, CA), 5 pockets (best druggability 0.58). MolNFT v1 #141377 on…
- PDB
- 5Z5H
- Type
- protein
- Length
- 504 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-xylosidase
- EC
- 3.2.1.37
- UniProt
- Q2I2N4
- Ligands
- XYS, CA
- Pockets
- 5 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-xylosidase (EC 3.2.1.37) | protein | 504 | 3% helix, 49% strand | Q2I2N4 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 280 | 0.58 | 0.78 | 21 | empty |
| 2 | 213 | 0.56 | 0.79 | 32 | XYS |
| 3 | 168 | 0.47 | 0.76 | 22 | empty |
| 4 | 165 | 0.47 | 0.76 | 29 | empty |
| 5 | 51 | 0.37 | 0.81 | 14 | empty |
Compared structures
- 5Z5H · Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase… · 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 Q2I2N4
- Elsewhere: RCSB PDB 5Z5H · PDBe 5Z5H · UniProt Q2I2N4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.