Research workbench
Structure of the class II fructose-1,6-bisphophatase from francisella tularensis
Analyse Structure of the class II fructose-1,6-bisphophatase from francisella tularensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JS3
- Type
- protein
- Length
- 1,300 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0E2ZJY0
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 325 | — | A0A0E2ZJY0 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B, C
- GOL · Glycerol · additive · 6 copies · chains A, B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7JS3 · Structure of the Class II Fructose-1,6-Bisphophatase from Francisella tularensis · 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 A0A0E2ZJY0
- Elsewhere: RCSB PDB 7JS3 · PDBe 7JS3 · UniProt A0A0E2ZJY0
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