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9RVA

Crystal structure of the extracellular part of human ACE2 in complex with the macrocyclic peptide WJL-63

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0001618molecular_functionvirus receptor activity
A0001817biological_processregulation of cytokine production
A0002003biological_processangiotensin maturation
A0003051biological_processangiotensin-mediated drinking behavior
A0003081biological_processregulation of systemic arterial blood pressure by renin-angiotensin
A0004175molecular_functionendopeptidase activity
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005788cellular_componentendoplasmic reticulum lumen
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0008237molecular_functionmetallopeptidase activity
A0008241molecular_functionpeptidyl-dipeptidase activity
A0008270molecular_functionzinc ion binding
A0009986cellular_componentcell surface
A0015827biological_processtryptophan transport
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0019058biological_processviral life cycle
A0019065biological_processreceptor-mediated endocytosis of virus by host cell
A0019229biological_processregulation of vasoconstriction
A0030666cellular_componentendocytic vesicle membrane
A0031526cellular_componentbrush border membrane
A0042127biological_processregulation of cell population proliferation
A0042802molecular_functionidentical protein binding
A0045121cellular_componentmembrane raft
A0046718biological_processsymbiont entry into host cell
A0046813biological_processreceptor-mediated virion attachment to host cell
A0048662biological_processnegative regulation of smooth muscle cell proliferation
A0050727biological_processregulation of inflammatory response
A0051957biological_processpositive regulation of amino acid transport
A0060135biological_processmaternal process involved in female pregnancy
A0060452biological_processpositive regulation of cardiac muscle contraction
A0061025biological_processmembrane fusion
A0070062cellular_componentextracellular exosome
A0070373biological_processnegative regulation of ERK1 and ERK2 cascade
A0089718biological_processamino acid import across plasma membrane
A0097746biological_processblood vessel diameter maintenance
A0098670biological_processentry receptor-mediated virion attachment to host cell
A0141109molecular_functiontransporter activator activity
A1902495cellular_componenttransmembrane transporter complex
A1903598biological_processpositive regulation of gap junction assembly
A1903779biological_processregulation of cardiac conduction
A1905737biological_processpositive regulation of L-proline import across plasma membrane
A2000379biological_processpositive regulation of reactive oxygen species metabolic process
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
ATHR371-GLN380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues588
DetailsDomain: {"description":"Peptidase M2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues17
DetailsRegion: {"description":"Interaction with SARS-CoV spike glycoprotein","evidences":[{"source":"PubMed","id":"15791205","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsRegion: {"description":"Essential for cleavage by ADAM17","evidences":[{"source":"PubMed","id":"24227843","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive 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"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19021774","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

255239

PDB entries from 2026-06-17

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