8Y8S
Cryo-EM structure of AQP3 in DMPC nanodisc
Functional Information from PROSITE/UniProt
site_id | PS00221 |
Number of Residues | 9 |
Details | MIP MIP family signature. HLNPAVTFA |
Chain | Residue | Details |
A | HIS81-ALA89 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 284 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:O14520 |
Chain | Residue | Details |
A | MET1-GLN24 | |
B | ILE265-ILE292 | |
C | MET1-GLN24 | |
C | GLY75-SER78 | |
C | LEU93-LYS100 | |
C | ILE178-GLY189 | |
C | ILE265-ILE292 | |
D | MET1-GLN24 | |
D | GLY75-SER78 | |
D | LEU93-LYS100 | |
D | ILE178-GLY189 | |
A | GLY75-SER78 | |
D | ILE265-ILE292 | |
A | LEU93-LYS100 | |
A | ILE178-GLY189 | |
A | ILE265-ILE292 | |
B | MET1-GLN24 | |
B | GLY75-SER78 | |
B | LEU93-LYS100 | |
B | ILE178-GLY189 |
site_id | SWS_FT_FI2 |
Number of Residues | 68 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000250|UniProtKB:O14520 |
Chain | Residue | Details |
A | ALA25-SER42 | |
B | ALA25-SER42 | |
C | ALA25-SER42 | |
D | ALA25-SER42 |
site_id | SWS_FT_FI3 |
Number of Residues | 280 |
Details | TOPO_DOM: Extracellular => ECO:0000250|UniProtKB:O14520 |
Chain | Residue | Details |
A | VAL43-PHE56 | |
C | LEU122-ASN159 | |
C | GLY207-SER210 | |
C | PHE225-TRP242 | |
D | VAL43-PHE56 | |
D | LEU122-ASN159 | |
D | GLY207-SER210 | |
D | PHE225-TRP242 | |
A | LEU122-ASN159 | |
A | GLY207-SER210 | |
A | PHE225-TRP242 | |
B | VAL43-PHE56 | |
B | LEU122-ASN159 | |
B | GLY207-SER210 | |
B | PHE225-TRP242 | |
C | VAL43-PHE56 |
site_id | SWS_FT_FI4 |
Number of Residues | 68 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000250|UniProtKB:O14520 |
Chain | Residue | Details |
A | LEU57-ALA74 | |
B | LEU57-ALA74 | |
C | LEU57-ALA74 | |
D | LEU57-ALA74 |
site_id | SWS_FT_FI5 |
Number of Residues | 104 |
Details | INTRAMEM: Discontinuously helical => ECO:0000250|UniProtKB:O14520 |
Chain | Residue | Details |
A | GLY79-PHE92 | |
A | GLY211-LEU224 | |
B | GLY79-PHE92 | |
B | GLY211-LEU224 | |
C | GLY79-PHE92 | |
C | GLY211-LEU224 | |
D | GLY79-PHE92 | |
D | GLY211-LEU224 |
site_id | SWS_FT_FI6 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000250|UniProtKB:O14520 |
Chain | Residue | Details |
A | LEU101-GLY121 | |
B | LEU101-GLY121 | |
C | LEU101-GLY121 | |
D | LEU101-GLY121 |
site_id | SWS_FT_FI7 |
Number of Residues | 68 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:O14520 |
Chain | Residue | Details |
A | GLY160-ALA177 | |
B | GLY160-ALA177 | |
C | GLY160-ALA177 | |
D | GLY160-ALA177 |
site_id | SWS_FT_FI8 |
Number of Residues | 64 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:O14520 |
Chain | Residue | Details |
A | LEU190-MET206 | |
B | LEU190-MET206 | |
C | LEU190-MET206 | |
D | LEU190-MET206 |
site_id | SWS_FT_FI9 |
Number of Residues | 84 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:O14520 |
Chain | Residue | Details |
A | TRP243-MET264 | |
B | TRP243-MET264 | |
C | TRP243-MET264 | |
D | TRP243-MET264 |
site_id | SWS_FT_FI10 |
Number of Residues | 12 |
Details | SITE: Selectivity filter => ECO:0000250|UniProtKB:O14520 |
Chain | Residue | Details |
A | PHE63 | |
D | PHE63 | |
D | TYR212 | |
D | ARG218 | |
A | TYR212 | |
A | ARG218 | |
B | PHE63 | |
B | TYR212 | |
B | ARG218 | |
C | PHE63 | |
C | TYR212 | |
C | ARG218 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN141 | |
B | ASN141 | |
C | ASN141 | |
D | ASN141 |