Research workbench
Complex structure of GH113 beta-1,4-mannanase
Analyse Complex structure of GH113 beta-1,4-mannanase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YLI
- Type
- protein
- Length
- 618 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- K0J0N5
- Ligands
- BMA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | — | protein | 309 | — | K0J0N5 |
Ligands and binding sites
- BMA · beta-D-mannopyranose · sugar · 8 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5YLI · Complex structure of GH113 beta-1,4-mannanase · the same entry in another collection · chain B against B, 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 K0J0N5
- Elsewhere: RCSB PDB 5YLI · PDBe 5YLI · UniProt K0J0N5
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