Research workbench
Difructose dianhydride I SYNTHASE/HYDROLASE (ALPHAFFASE1) from bifidobacterium dentium in complex with beta-D-fructofuranose
Analyse Difructose dianhydride I SYNTHASE/HYDROLASE (ALPHAFFASE1) from bifidobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V1X
- Type
- protein
- Length
- 2,682 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A6L9SN29
- Ligands
- FRU, CA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 447 | — | A0A6L9SN29 |
Ligands and binding sites
- FRU · beta-D-fructofuranose · sugar · 6 copies · chains A, D, B, C, F, E
- CA · Calcium ion · metal · 6 copies · chains A, D, B, C, F, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7V1X · Difructose dianhydride I synthase/hydrolase (alphaFFase1) from Bifidobacterium dentium 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 A0A6L9SN29
- Elsewhere: RCSB PDB 7V1X · PDBe 7V1X · UniProt A0A6L9SN29
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