MolNFT v1 · #47389 · protein
R-state, pep and fru-6-P-bound, escherichia COLI fructose-1,6- bisphosphatase
2OX3 · Fructose-1,6-bisphosphatase: “R-state, pep and fru-6-P-bound, escherichia COLI fructose-1,6- bisphosphatase”. X-ray diffraction, 2 ligands (F6P, PEP), 2 pockets (best druggability 0.40). MolNFT v1 #47389 on GenesisL1: 3D structure…
- PDB
- 2OX3
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphatase
- EC
- 3.1.3.11
- UniProt
- P0A993
- Ligands
- F6P, PEP
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 315 | 37% helix, 24% strand | P0A993 |
Ligands and binding sites
- F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · chains A
- PEP · Phosphoenolpyruvate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.40 | 0.77 | 21 | F6P |
| 2 | 84 | 0.36 | 0.76 | 21 | empty |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 2OX3 · R-state, PEP and Fru-6-P-bound, Escherichia coli fructose-1,6-bisphosphatase · the same entry in another collection · chain A against A, TM-score 1.00
- P0A993 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase class 1 (P0A993) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P0A993
- Elsewhere: RCSB PDB 2OX3 · PDBe 2OX3 · UniProt P0A993
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