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Structure of the catalytic domain of the bacillus circulans alpha-1,6 mannanase in complex with an alpha-1,6-alpha-manno-cyclophellitol trisaccharide inhibitor
Analyse Structure of the catalytic domain of the bacillus circulans alpha-1,6 mannanase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NL5
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9Z4P9
- Ligands
- UKQ, UKT, MAN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 335 | — | Q9Z4P9 |
Ligands and binding sites
- UKQ · (1R,6S)-5beta-(Hydroxymethyl)-7-oxabicyclo[4.1.0]heptane-2beta,3beta,4alpha-triol · ligand · chains A
- UKT · (1R,2R,3R,4S,5R)-4-(hydroxymethyl)cyclohexane-1,2,3,5-tetrol · ligand · chains A
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NL5 · Structure of the catalytic domain of the Bacillus circulans alpha-1,6 Mannanase in… · 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 Q9Z4P9
- Elsewhere: RCSB PDB 7NL5 · PDBe 7NL5 · UniProt Q9Z4P9
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