Research workbench
Apo structure of beta-1,3-1,4-glucanase from paenibacillus SP.X4
Analyse Apo structure of beta-1,3-1,4-glucanase from paenibacillus SP.X4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XD0
- Type
- protein
- Length
- 756 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucanase
- EC
- 3.2.1.73
- UniProt
- A0A088BCU2
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glucanase (EC 3.2.1.73) | protein | 378 | 50% helix, 8% strand | A0A088BCU2 |
Ligands and binding sites
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 | 240 | 0.55 | 0.77 | 31 | PEG |
| 2 | 275 | 0.53 | 0.75 | 39 | empty |
| 3 | 207 | 0.53 | 0.77 | 27 | PGE |
Interfaces
1 interface between chains.
- A–B · 414 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5XD0 · Apo Structure of Beta-1,3-1,4-glucanase from Paenibacillus sp.X4 · 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 A0A088BCU2
- Elsewhere: RCSB PDB 5XD0 · PDBe 5XD0 · UniProt A0A088BCU2
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