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Crystal structure of endo-beta-1,4-mannanase from the alkaliphilic bacillus sp. N16-5
Analyse Crystal structure of endo-beta-1,4-mannanase from the alkaliphilic bacillus sp.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JUG
- Type
- protein
- Length
- 294 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-mannanase
- EC
- 3.2.1.78
- UniProt
- Q5YEX6
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-mannanase (EC 3.2.1.78) | protein | 294 | 39% helix, 18% strand | Q5YEX6 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 179 | 0.50 | 0.77 | 24 | empty |
Compared structures
- 3JUG · Crystal structure of endo-beta-1,4-mannanase from the alkaliphilic Bacillus sp. N16-5 · 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 Q5YEX6
- Elsewhere: RCSB PDB 3JUG · PDBe 3JUG · UniProt Q5YEX6
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