Research workbench
Native bacillus subtilis arabinanase ARB43A
Analyse Native bacillus subtilis arabinanase ARB43A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UV4
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arabinan-endo 1,5-alpha-L-arabinase
- EC
- 3.2.1.99
- UniProt
- P94522
- Ligands
- CA
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arabinan-endo 1,5-alpha-L-arabinase (EC 3.2.1.99) | protein | 291 | 3% helix, 53% strand | P94522 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 261 | 0.57 | 0.78 | 30 | empty |
| 2 | 70 | 0.38 | 0.78 | 20 | EDO |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P94522
- Elsewhere: RCSB PDB 1UV4 · PDBe 1UV4 · UniProt P94522
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