×
Network disruptions
We have been experiencing disruptions on our local network which has affected the stability of these web pages.
We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.
PDB Information
| PDB | 3DFP |
| Method | X-RAY DIFFRACTION |
| Host Organism | Escherichia coli |
| Gene Source | Oryctolagus cuniculus |
| Primary Citation |
Charge stabilization and entropy reduction of central lysine residues in fructose-bisphosphate aldolase
St-Jean, M., Blonski, C., Sygusch, J.
Biochemistry
|
| Header | Lyase |
| Released | 2008-06-12 |
| Resolution | 2.050 |
| CATH Insert Date | 16 Aug, 2009 |
PDB Images (9)
3dfpA00
CATH Domain 3dfpA00
3dfpB00
CATH Domain 3dfpB00
3dfpC00
CATH Domain 3dfpC00
3dfpD00
CATH Domain 3dfpD00
PDB Chains (4)
CATH Domains (4)
UniProtKB Entries (4)
| Accession |
Gene ID |
Taxon |
Description |
| P00883 |
ALDOA_RABIT |
Oryctolagus cuniculus |
Fructose-bisphosphate aldolase A |
| P00883 |
ALDOA_RABIT |
Oryctolagus cuniculus |
Fructose-bisphosphate aldolase A |
| P00883 |
ALDOA_RABIT |
Oryctolagus cuniculus |
Fructose-bisphosphate aldolase A |
| P00883 |
ALDOA_RABIT |
Oryctolagus cuniculus |
Fructose-bisphosphate aldolase A |