×
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 | 1J4E |
| Method | X-RAY DIFFRACTION |
| Host Organism | Escherichia coli |
| Gene Source | Oryctolagus cuniculus |
| Primary Citation |
Snapshots of catalysis: the structure of fructose-1,6-(bis)phosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate.
Choi, K.H., Shi, J., Hopkins, C.E., Tolan, D.R., Allen, K.N.
Biochemistry
|
| Header | Lyase |
| Released | 2001-09-19 |
| Resolution | 2.650 |
| CATH Insert Date | 05 Mar, 2006 |
PDB Images (9)
1j4eA00
CATH Domain 1j4eA00
1j4eB00
CATH Domain 1j4eB00
1j4eC00
CATH Domain 1j4eC00
1j4eD00
CATH Domain 1j4eD00
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 |