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Structure of the GH99 endo-alpha-mannanase from bacteroides xylanisolvens in complex with alpha-glc-1,3-1,2-anhydro-mannose hydrolyzed by enzyme
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
- 6FWM
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D6D1V7
- Ligands
- M96, GLC
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 349 | — | D6D1V7 |
Ligands and binding sites
- M96 · (1~{S},2~{R},3~{S},4~{R},5~{R})-5-(hydroxymethyl) cyclohexane-1,2,3,4-tetrol · ligand · chains A
- GLC · alpha-D-glucopyranose · sugar · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FWM · 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 6FWM · PDBe 6FWM · UniProt D6D1V7
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