6DO1
Structure of nanobody-stabilized angiotensin II type 1 receptor bound to S1I8
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 |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0004945 | molecular_function | angiotensin type II receptor activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016020 | cellular_component | membrane |
| B | 0019229 | biological_process | regulation of vasoconstriction |
| B | 0020037 | molecular_function | heme binding |
| B | 0022900 | biological_process | electron transport chain |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
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 | 58 |
| 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 | |
| B | TYR26-PHE55 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| 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 | |
| B | TYR56-THR61 | |
| B | ARG126-THR141 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 54 |
| 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 | |
| B | VAL62-ALA89 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 64 |
| 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 | |
| B | MET90-ASN98 | |
| B | HIS166-THR190 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 52 |
| 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 | |
| B | TYR99-ASP125 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 46 |
| 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 | |
| B | MET142-ILE165 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 50 |
| 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 | |
| B | LEU191-THR216 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 56 |
| 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 | LYS339-LEU367 | |
| B | LYS339-LEU367 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 18 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD |
| Chain | Residue | Details |
| A | GLY368-ASP377 | |
| B | GLY368-ASP377 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 50 |
| 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 | ILE378-PHE403 | |
| B | ILE378-PHE403 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:30639100, ECO:0007744|PDB:6DO1 |
| Chain | Residue | Details |
| A | GLN15 | |
| B | GLN15 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:30639100, ECO:0000305|PubMed:32079768, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0 |
| Chain | Residue | Details |
| A | ASP17 | |
| B | HIS183 | |
| B | TYR184 | |
| B | LYS199 | |
| A | ARG167 | |
| A | PHE182 | |
| A | HIS183 | |
| A | TYR184 | |
| A | LYS199 | |
| B | ASP17 | |
| B | ARG167 | |
| B | PHE182 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19139490 |
| Chain | Residue | Details |
| A | ASN4 | |
| B | ASN4 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| 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 | |
| B | ASN176 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN188 | |
| B | ASN188 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | TRP232 | |
| B | TRP232 |
