6VK0
CryoEM structure of Hrd1-Usa1/Der1/Hrd3 of the flipped topology
Functional Information from GO Data
Chain | GOid | namespace | contents |
C | 0000836 | cellular_component | Hrd1p ubiquitin ligase complex |
C | 0000839 | cellular_component | Hrd1p ubiquitin ligase ERAD-L complex |
C | 0005047 | molecular_function | signal recognition particle binding |
C | 0005515 | molecular_function | protein binding |
C | 0005783 | cellular_component | endoplasmic reticulum |
C | 0005789 | cellular_component | endoplasmic reticulum membrane |
C | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
C | 0006950 | biological_process | response to stress |
C | 0015031 | biological_process | protein transport |
C | 0016020 | cellular_component | membrane |
C | 0030968 | biological_process | endoplasmic reticulum unfolded protein response |
C | 0030970 | biological_process | retrograde protein transport, ER to cytosol |
C | 0036503 | biological_process | ERAD pathway |
C | 0051787 | molecular_function | misfolded protein binding |
C | 0070843 | biological_process | misfolded protein transport |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 101 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:32327568 |
Chain | Residue | Details |
B | MET1-LYS8 | |
B | GLY72-GLU84 | |
B | ASP127-PHE147 | |
B | LEU209-GLU271 | |
A | ASN611 |
site_id | SWS_FT_FI2 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:32327568 |
Chain | Residue | Details |
B | GLN9-LYS30 |
site_id | SWS_FT_FI3 |
Number of Residues | 29 |
Details | TOPO_DOM: Lumenal => ECO:0000269|PubMed:32327568 |
Chain | Residue | Details |
B | THR31-ASN43 | |
B | GLU102-ARG103 | |
B | SER170-THR183 | |
B | PHE293-PRO296 |
site_id | SWS_FT_FI4 |
Number of Residues | 27 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:32327568 |
Chain | Residue | Details |
B | GLU44-PHE71 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:32327568 |
Chain | Residue | Details |
B | ARG85-HIS101 |
site_id | SWS_FT_FI6 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:32327568 |
Chain | Residue | Details |
B | TYR104-LYS126 |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:32327568 |
Chain | Residue | Details |
B | SER148-ILE169 |
site_id | SWS_FT_FI8 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:32327568 |
Chain | Residue | Details |
B | SER184-CYS208 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:32327568 |
Chain | Residue | Details |
B | LYS272-PRO292 |
site_id | SWS_FT_FI10 |
Number of Residues | 17 |
Details | TRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:32327568 |
Chain | Residue | Details |
B | MET297-GLY314 |
site_id | SWS_FT_FI11 |
Number of Residues | 51 |
Details | ZN_FING: RING-type; atypical => ECO:0000255|PROSITE-ProRule:PRU00175 |
Chain | Residue | Details |
B | CYS349-ARG400 |