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Structure of the GH99 endo-alpha-mannanase from bacteroides xylanisolvens in complex with mannose-alpha-1,3-noeuromycin
Analyse Structure of the GH99 endo-alpha-mannanase from bacteroides xylanisolvens in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LYR
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D6D1V7
- Ligands
- MNM, MAN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 349 | — | D6D1V7 |
Ligands and binding sites
- MNM · (2S,3S,4R,5R)-2,3,4-trihydroxy-5-hydroxymethyl-piperidine · ligand · chains A
- MAN · alpha-D-mannopyranose · sugar · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5LYR · Structure of the GH99 endo-alpha-mannanase from Bacteroides xylanisolvens in complex with… · 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 D6D1V7
- Elsewhere: RCSB PDB 5LYR · PDBe 5LYR · UniProt D6D1V7
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