9AVG
Structure of human calcium-sensing receptor in complex with chimeric Gs (miniGis) protein in nanodiscs
This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_id | PS00678 |
Number of Residues | 15 |
Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS |
Chain | Residue | Details |
B | LEU70-SER84 | |
B | ILE157-ILE171 | |
B | LEU285-ALA299 |
site_id | PS00979 |
Number of Residues | 19 |
Details | G_PROTEIN_RECEP_F3_1 G-protein coupled receptors family 3 signature 1. VaNLLgLFyIPQVSyASSS |
Chain | Residue | Details |
Q | VAL153-SER171 |
site_id | PS00980 |
Number of Residues | 25 |
Details | G_PROTEIN_RECEP_F3_2 G-protein coupled receptors family 3 signature 2. CCFeCveCpdgeYsdet.DasACnkC |
Chain | Residue | Details |
Q | CYS561-CYS585 |
site_id | PS00981 |
Number of Residues | 11 |
Details | G_PROTEIN_RECEP_F3_3 G-protein coupled receptors family 3 signature 3. FNEAKfITFSM |
Chain | Residue | Details |
Q | PHE801-MET811 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
Q | GLU671-GLN681 | |
Q | ALA746-SER769 | |
Q | TYR829-VAL836 | |
R | TYR20-PHE612 | |
R | GLU671-GLN681 | |
R | ALA746-SER769 | |
R | TYR829-VAL836 | |
G | ALA2 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Cysteine methyl ester => ECO:0000250|UniProtKB:P63212 |
Chain | Residue | Details |
R | GLY613-ILE635 | |
G | CYS68 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | LIPID: S-geranylgeranyl cysteine => ECO:0000250|UniProtKB:P63212 |
Chain | Residue | Details |
Q | ARG701-GLN724 | |
Q | LYS793-LYS805 | |
R | LYS636-GLU649 | |
R | ARG701-GLN724 | |
R | LYS793-LYS805 | |
G | CYS68 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824 |
Chain | Residue | Details |
R | LEU650-GLY670 | |
A | CYS3 |
site_id | SWS_FT_FI5 |
Number of Residues | 36 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
Q | PRO682-ASN700 | |
R | PRO682-ASN700 |
site_id | SWS_FT_FI6 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
Q | PHE725-THR745 | |
R | PHE725-THR745 |
site_id | SWS_FT_FI7 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
Q | LEU770-PHE792 | |
R | LEU770-PHE792 |
site_id | SWS_FT_FI8 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
Q | PHE806-THR828 | |
R | PHE806-THR828 |
site_id | SWS_FT_FI9 |
Number of Residues | 50 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
Q | GLU837-PHE862 | |
R | GLU837-PHE862 |
site_id | SWS_FT_FI10 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27434672, ECO:0007744|PDB:5K5S |
Chain | Residue | Details |
Q | ARG66 | |
R | ASP234 | |
R | ARG415 | |
R | GLY557 | |
Q | THR145 | |
Q | GLU231 | |
Q | ASP234 | |
Q | ARG415 | |
Q | GLY557 | |
R | ARG66 | |
R | THR145 | |
R | GLU231 |
site_id | SWS_FT_FI11 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27434672, ECO:0000305|PubMed:27386547, ECO:0007744|PDB:5FBH, ECO:0007744|PDB:5FBK, ECO:0007744|PDB:5K5S |
Chain | Residue | Details |
Q | ILE81 | |
Q | LEU87 | |
Q | LEU88 | |
R | ILE81 | |
R | LEU87 | |
R | LEU88 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27434672, ECO:0000305|PubMed:27386547, ECO:0007744|PDB:5FBK, ECO:0007744|PDB:5K5S |
Chain | Residue | Details |
Q | SER84 | |
R | SER84 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27434672, ECO:0007744|PDB:5K5S, ECO:0007744|PDB:5K5T |
Chain | Residue | Details |
Q | THR100 | |
R | THR100 |
site_id | SWS_FT_FI14 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27386547, ECO:0000269|PubMed:27434672, ECO:0007744|PDB:5FBH, ECO:0007744|PDB:5FBK, ECO:0007744|PDB:5K5S |
Chain | Residue | Details |
Q | SER147 | |
Q | ALA168 | |
Q | SER170 | |
Q | GLU297 | |
R | SER147 | |
R | ALA168 | |
R | SER170 | |
R | GLU297 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | SITE: Important for ability of agonist AMG 416 to activate G-protein-coupled receptor activity => ECO:0000269|PubMed:26290606 |
Chain | Residue | Details |
Q | CYS482 | |
R | CYS482 |
site_id | SWS_FT_FI16 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
Q | ASN90 | |
Q | ASN130 | |
Q | ASN386 | |
Q | ASN400 | |
R | ASN90 | |
R | ASN130 | |
R | ASN386 | |
R | ASN400 |
site_id | SWS_FT_FI17 |
Number of Residues | 14 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:27434672 |
Chain | Residue | Details |
Q | ASN261 | |
R | ASN446 | |
R | ASN468 | |
R | ASN488 | |
R | ASN541 | |
R | ASN594 | |
Q | ASN287 | |
Q | ASN446 | |
Q | ASN468 | |
Q | ASN488 | |
Q | ASN541 | |
Q | ASN594 | |
R | ASN261 | |
R | ASN287 |