6VK0
CryoEM structure of Hrd1-Usa1/Der1/Hrd3 of the flipped topology
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 41 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 38 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"32327568","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 72 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"32327568","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"32327568","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 60 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"32327568","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 32 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"32327568","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 37 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"32327568","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 36 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"32327568","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"32327568","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 36 |
| Details | Repeat: {"description":"Sel1-like 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 35 |
| Details | Repeat: {"description":"Sel1-like 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 32 |
| Details | Repeat: {"description":"Sel1-like 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 43 |
| Details | Repeat: {"description":"Sel1-like 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 31 |
| Details | Repeat: {"description":"Sel1-like 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 35 |
| Details | Repeat: {"description":"Sel1-like 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 5 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"32327568","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 17 |
| Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"32327568","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
