Research workbench
GH127 beta-L-arabinofuranosidase HYPBA1 E322Q mutant complexed with P- nitrophenyl beta-L-arabinofuranoside
Analyse GH127 beta-L-arabinofuranosidase HYPBA1 E322Q mutant complexed with P… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EXU
- Type
- protein
- Length
- 651 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
- 07Y, ZN
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-reducing end beta-L-arabinofuranosidase (EC 3.2.1.185) | protein | 651 | 40% helix, 17% strand | E8MGH8 |
Ligands and binding sites
- 07Y · (2S,3R,4R,5R)-2-(hydroxymethyl)-5-(4-nitrophenoxy) oxolane-3,4-diol · ligand · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 359 | 0.65 | 0.80 | 36 | empty |
| 2 | 247 | 0.62 | 0.81 | 37 | 07Y |
| 3 | 338 | 0.59 | 0.76 | 37 | empty |
Compared structures
- 7EXU · GH127 beta-L-arabinofuranosidase HypBA1 E322Q mutant complexed with p-nitrophenyl… · the same entry in another collection · chain A against A, TM-score 1.00
- E8MGH8 · AlphaFold monomer V2.0 prediction for non-reducing end beta-L- arabinofuranosidase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 7EXU · PDBe 7EXU · UniProt E8MGH8
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