Research workbench
Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase
Analyse Crystallographic studies of the catalytic mechanism of the neutral form of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FBC
- Type
- protein
- Length
- 626 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose 1,6-bisphosphatase
- EC
- 3.1.3.11
- UniProt
- P00636
- Ligands
- AHG, MG
- Pockets
- 9 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose 1,6-bisphosphatase (EC 3.1.3.11) | protein | 312 | 36% helix, 27% strand | P00636 |
| B | Fructose 1,6-bisphosphatase (EC 3.1.3.11) | protein | 314 | 39% helix, 27% strand | P00636 |
Ligands and binding sites
- AHG · 2,5-anhydro-1,6-di-O-phosphono-D-glucitol · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 234 | 0.56 | 0.78 | 38 | AHG |
| 2 | 138 | 0.50 | 0.80 | 21 | AHG |
| 3 | 152 | 0.46 | 0.77 | 24 | empty |
| 4 | 115 | 0.46 | 0.79 | 21 | empty |
| 5 | 72 | 0.38 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1992 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1FBC · Crystallographic studies of the catalytic mechanism of the neutral form of… · the same entry in another collection · chain A against A, TM-score 1.00
- P00636 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 (P00636) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00636
- Elsewhere: RCSB PDB 1FBC · PDBe 1FBC · UniProt P00636
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