×
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 | 5FER |
| Method | X-RAY DIFFRACTION |
| Host Organism | Escherichia coli |
| Gene Source | Homo sapiens |
| Primary Citation |
Functional role of TRIM E3 ligase oligomerization and regulation of catalytic activity.
Koliopoulos, M.G., Esposito, D., Christodoulou, E., Taylor, I.A., Rittinger, K.
Embo J.
|
| Header | Ligase |
| Released | 2015-12-17 |
| Resolution | 2.340 |
| CATH Insert Date | 29 May, 2016 |
PDB Images (13)
5ferA00
CATH Domain 5ferA00
5ferB00
CATH Domain 5ferB00
5ferC00
CATH Domain 5ferC00
5ferD00
CATH Domain 5ferD00
5ferE00
CATH Domain 5ferE00
5ferF00
CATH Domain 5ferF00
PDB Chains (6)
CATH Domains (6)
UniProtKB Entries (6)
| Accession |
Gene ID |
Taxon |
Description |
| P62992 |
RS27A_BOVIN |
Bos taurus |
Ubiquitin-40S ribosomal protein S27a |
| P51668 |
UB2D1_HUMAN |
Homo sapiens |
Ubiquitin-conjugating enzyme E2 D1 |
| P62992 |
RS27A_BOVIN |
Bos taurus |
Ubiquitin-40S ribosomal protein S27a |
| Q14258 |
TRI25_HUMAN |
Homo sapiens |
E3 ubiquitin/ISG15 ligase TRIM25 |
| P51668 |
UB2D1_HUMAN |
Homo sapiens |
Ubiquitin-conjugating enzyme E2 D1 |
| Q14258 |
TRI25_HUMAN |
Homo sapiens |
E3 ubiquitin/ISG15 ligase TRIM25 |