Research workbench
Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate-binding module
Analyse Structural and thermodynamic dissection of specific mannan recognition by a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OH4
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-mannosidase
- UniProt
- Q9RIK9
- Ligands
- BMA, GLA, CA, SO4
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-mannosidase | protein | 174 | 6% helix, 59% strand | Q9RIK9 |
Ligands and binding sites
- BMA · beta-D-mannopyranose · sugar · 5 copies · chains A
- GLA · alpha-D-galactopyranose · sugar · 2 copies · chains A
- CA · Calcium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1OH4 · Structural and thermodynamic dissection of specific mannan recognition by a… · 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 Q9RIK9
- Elsewhere: RCSB PDB 1OH4 · PDBe 1OH4 · UniProt Q9RIK9
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