6OS1
Structure of synthetic nanobody-stabilized angiotensin II type 1 receptor bound to TRV023
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0004945 | molecular_function | angiotensin type II receptor activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0009055 | molecular_function | electron transfer activity |
A | 0016020 | cellular_component | membrane |
A | 0019229 | biological_process | regulation of vasoconstriction |
A | 0020037 | molecular_function | heme binding |
A | 0022900 | biological_process | electron transport chain |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue OLC A 1401 |
Chain | Residue |
A | CYS121 |
A | OLC1406 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue OLC A 1402 |
Chain | Residue |
A | MET1243 |
A | ALA1244 |
A | LEU1247 |
A | ASN1294 |
A | OLC1405 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue OLC A 1403 |
Chain | Residue |
A | LYS1310 |
A | LEU1268 |
A | PHE1304 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue OLC A 1404 |
Chain | Residue |
A | TRP219 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue OLC A 1405 |
Chain | Residue |
A | GLY194 |
A | OLC1402 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue OLC A 1406 |
Chain | Residue |
A | THR120 |
A | ILE151 |
A | OLC1401 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue CLR A 1407 |
Chain | Residue |
A | ILE51 |
A | LEU1316 |
Functional Information from PROSITE/UniProt
site_id | PS00237 |
Number of Residues | 17 |
Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVfLLTCLSIDRYLaI |
Chain | Residue | Details |
A | ALA114-ILE130 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 29 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100, ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1, ECO:0007744|PDB:6OS2 |
Chain | Residue | Details |
A | TYR26-PHE55 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100, ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1, ECO:0007744|PDB:6OS2 |
Chain | Residue | Details |
A | TYR56-THR61 | |
A | ARG126-THR141 |
site_id | SWS_FT_FI3 |
Number of Residues | 27 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100, ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1, ECO:0007744|PDB:6OS2 |
Chain | Residue | Details |
A | VAL62-ALA89 |
site_id | SWS_FT_FI4 |
Number of Residues | 32 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100, ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1, ECO:0007744|PDB:6OS2 |
Chain | Residue | Details |
A | MET90-ASN98 | |
A | HIS166-THR190 |
site_id | SWS_FT_FI5 |
Number of Residues | 26 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100, ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1, ECO:0007744|PDB:6OS2 |
Chain | Residue | Details |
A | TYR99-ASP125 |
site_id | SWS_FT_FI6 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100, ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1, ECO:0007744|PDB:6OS2 |
Chain | Residue | Details |
A | MET142-ILE165 |
site_id | SWS_FT_FI7 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0000269|PubMed:30639100, ECO:0000269|PubMed:32079768, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0, ECO:0007744|PDB:6OS1, ECO:0007744|PDB:6OS2 |
Chain | Residue | Details |
A | LEU191-THR216 |
site_id | SWS_FT_FI8 |
Number of Residues | 28 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD |
Chain | Residue | Details |
A | LYS1240-LEU1268 |
site_id | SWS_FT_FI9 |
Number of Residues | 9 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD |
Chain | Residue | Details |
A | GLY1269-ASP1278 |
site_id | SWS_FT_FI10 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD |
Chain | Residue | Details |
A | ILE1279-PHE1304 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:30639100, ECO:0007744|PDB:6DO1 |
Chain | Residue | Details |
A | GLN15 |
site_id | SWS_FT_FI12 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:30639100, ECO:0000305|PubMed:32079768, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0 |
Chain | Residue | Details |
A | ASP17 | |
A | ARG167 | |
A | PHE182 | |
A | HIS183 | |
A | TYR184 | |
A | LYS199 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19139490 |
Chain | Residue | Details |
A | ASN4 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30639100, ECO:0000269|PubMed:32079768, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0 |
Chain | Residue | Details |
A | ASN176 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN188 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | TRP232 |