Research workbench
R-state, citrate and fru-6-P-bound escherichia COLI fructose-1,6- bisphosphatase
Analyse R-state, citrate and fru-6-P-bound escherichia COLI fructose-1,6- bisphosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OWZ
- 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
- Pockets
- 3 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphatase (EC 3.1.3.11) | protein | 315 | 39% helix, 23% strand | P0A993 |
Ligands and binding sites
- F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · chains A
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 124 | 0.43 | 0.77 | 22 | F6P |
| 2 | 91 | 0.37 | 0.76 | 22 | empty |
| 3 | 50 | 0.33 | 0.78 | 14 | empty |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 2OWZ · R-state, citrate 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 2OWZ · PDBe 2OWZ · UniProt P0A993
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