8WBY
Cryo-EM structure of ACE2-B0AT1 complex with JX98
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006836 | biological_process | neurotransmitter transport |
| A | 0006865 | biological_process | amino acid transport |
| A | 0007584 | biological_process | response to nutrient |
| A | 0015171 | molecular_function | amino acid transmembrane transporter activity |
| A | 0015175 | molecular_function | neutral L-amino acid transmembrane transporter activity |
| A | 0015293 | molecular_function | symporter activity |
| A | 0015804 | biological_process | neutral amino acid transport |
| A | 0016020 | cellular_component | membrane |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0019058 | biological_process | viral life cycle |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0031526 | cellular_component | brush border membrane |
| A | 0035725 | biological_process | sodium ion transmembrane transport |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0089718 | biological_process | amino acid import across plasma membrane |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| B | 0016020 | cellular_component | membrane |
| C | 0006508 | biological_process | proteolysis |
| C | 0008237 | molecular_function | metallopeptidase activity |
| C | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| C | 0016020 | cellular_component | membrane |
| D | 0005515 | molecular_function | protein binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006836 | biological_process | neurotransmitter transport |
| D | 0006865 | biological_process | amino acid transport |
| D | 0007584 | biological_process | response to nutrient |
| D | 0015171 | molecular_function | amino acid transmembrane transporter activity |
| D | 0015175 | molecular_function | neutral L-amino acid transmembrane transporter activity |
| D | 0015293 | molecular_function | symporter activity |
| D | 0015804 | biological_process | neutral amino acid transport |
| D | 0016020 | cellular_component | membrane |
| D | 0016324 | cellular_component | apical plasma membrane |
| D | 0019058 | biological_process | viral life cycle |
| D | 0022857 | molecular_function | transmembrane transporter activity |
| D | 0031526 | cellular_component | brush border membrane |
| D | 0035725 | biological_process | sodium ion transmembrane transport |
| D | 0070062 | cellular_component | extracellular exosome |
| D | 0089718 | biological_process | amino acid import across plasma membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ |
| Chain | Residue | Details |
| B | THR371-GLN380 |
| site_id | PS00610 |
| Number of Residues | 15 |
| Details | NA_NEUROTRAN_SYMP_1 Sodium:neurotransmitter symporter family signature 1. WRFPYlcqsHGGGaF |
| Chain | Residue | Details |
| A | TRP56-PHE70 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 412 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 184 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=11","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=12","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9D687","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 12 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU01354","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 34 |
| Details | Region: {"description":"Interaction with SARS-CoV spike glycoprotein","evidences":[{"source":"PubMed","id":"15791205","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 14 |
| Details | Region: {"description":"Essential for cleavage by ADAM17","evidences":[{"source":"PubMed","id":"24227843","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 38 |
| Details | Region: {"description":"Essential for cleavage by TMPRSS11D and TMPRSS2","evidences":[{"source":"PubMed","id":"24227843","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27217402","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19021774","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI27 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19901337","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19901337","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






