Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8WM3

Cryo-EM structure of ACE2-SIT1 complex with tiagabine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005298	molecular_function	proline:sodium symporter activity
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0006865	biological_process	amino acid transport
A	0015171	molecular_function	amino acid transmembrane transporter activity
A	0015175	molecular_function	neutral L-amino acid transmembrane transporter activity
A	0015188	molecular_function	L-isoleucine transmembrane transporter activity
A	0015193	molecular_function	L-proline transmembrane transporter activity
A	0015199	molecular_function	amino-acid betaine transmembrane transporter activity
A	0015293	molecular_function	symporter activity
A	0015370	molecular_function	solute:sodium symporter activity
A	0015816	biological_process	glycine transport
A	0015824	biological_process	proline transport
A	0015838	biological_process	amino-acid betaine transport
A	0016020	cellular_component	membrane
A	0016324	cellular_component	apical plasma membrane
A	0022857	molecular_function	transmembrane transporter activity
A	0035725	biological_process	sodium ion transmembrane transport
A	0089718	biological_process	amino acid import across plasma membrane
A	0150104	biological_process	transport across blood-brain barrier
A	1903804	biological_process	glycine import across plasma membrane
A	1903806	biological_process	L-isoleucine import across plasma membrane
A	1904271	biological_process	L-proline import across plasma membrane
A	1905647	biological_process	proline 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	0005298	molecular_function	proline:sodium symporter activity
C	0005515	molecular_function	protein binding
C	0005886	cellular_component	plasma membrane
C	0006865	biological_process	amino acid transport
C	0015171	molecular_function	amino acid transmembrane transporter activity
C	0015175	molecular_function	neutral L-amino acid transmembrane transporter activity
C	0015188	molecular_function	L-isoleucine transmembrane transporter activity
C	0015193	molecular_function	L-proline transmembrane transporter activity
C	0015199	molecular_function	amino-acid betaine transmembrane transporter activity
C	0015293	molecular_function	symporter activity
C	0015370	molecular_function	solute:sodium symporter activity
C	0015816	biological_process	glycine transport
C	0015824	biological_process	proline transport
C	0015838	biological_process	amino-acid betaine transport
C	0016020	cellular_component	membrane
C	0016324	cellular_component	apical plasma membrane
C	0022857	molecular_function	transmembrane transporter activity
C	0035725	biological_process	sodium ion transmembrane transport
C	0089718	biological_process	amino acid import across plasma membrane
C	0150104	biological_process	transport across blood-brain barrier
C	1903804	biological_process	glycine import across plasma membrane
C	1903806	biological_process	L-isoleucine import across plasma membrane
C	1904271	biological_process	L-proline import across plasma membrane
C	1905647	biological_process	proline import across plasma membrane
D	0006508	biological_process	proteolysis
D	0008237	molecular_function	metallopeptidase activity
D	0008241	molecular_function	peptidyl-dipeptidase activity
D	0016020	cellular_component	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. WRFPYlcqmYGGGsF

Chain	Residue	Details
A	TRP29-PHE43

site_id	PS00754
Number of Residues	21
Details	NA_NEUROTRAN_SYMP_2 Sodium:neurotransmitter symporter family signature 2. YLfhSFQdpLPWsvCplngNH

Chain	Residue	Details
A	TYR112-HIS132

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	470
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	144
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=11","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=12","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	40
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU01354","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
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_FI17
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_FI18
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_FI19
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_FI20
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_FI21
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_FI22
Number of Residues	6
Details	Binding site: {"evidences":[{"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
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_FI25
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_FI26
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_FI27
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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)