8Z3S
Activation mechanism and novel binding site of the BKCa channel activator CTIBD
This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
| site_id | PS00092 |
| Number of Residues | 7 |
| Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. VITNPPY |
| Chain | Residue | Details |
| A | VAL1091-TYR1097 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S0 => ECO:0000255 |
| Chain | Residue | Details |
| A | TRP22-LEU42 | |
| B | TRP22-LEU42 | |
| C | TRP22-LEU42 | |
| D | TRP22-LEU42 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 348 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| A | TRP43-ARG113 | |
| D | TRP43-ARG113 | |
| D | ALA171-LYS174 | |
| D | LEU221-LEU235 | |
| A | ALA171-LYS174 | |
| A | LEU221-LEU235 | |
| B | TRP43-ARG113 | |
| B | ALA171-LYS174 | |
| B | LEU221-LEU235 | |
| C | TRP43-ARG113 | |
| C | ALA171-LYS174 | |
| C | LEU221-LEU235 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S1 => ECO:0000255 |
| Chain | Residue | Details |
| A | VAL114-SER134 | |
| B | VAL114-SER134 | |
| C | VAL114-SER134 | |
| D | VAL114-SER134 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 152 |
| Details | TOPO_DOM: Extracellular => ECO:0000255 |
| Chain | Residue | Details |
| A | SER135-THR149 | |
| C | SER196-LEU199 | |
| C | GLU257-GLN270 | |
| C | TYR294-LEU302 | |
| D | SER135-THR149 | |
| D | SER196-LEU199 | |
| D | GLU257-GLN270 | |
| D | TYR294-LEU302 | |
| A | SER196-LEU199 | |
| A | GLU257-GLN270 | |
| A | TYR294-LEU302 | |
| B | SER135-THR149 | |
| B | SER196-LEU199 | |
| B | GLU257-GLN270 | |
| B | TYR294-LEU302 | |
| C | SER135-THR149 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S2 => ECO:0000255 |
| Chain | Residue | Details |
| A | LEU150-ALA170 | |
| B | LEU150-ALA170 | |
| C | LEU150-ALA170 | |
| D | LEU150-ALA170 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S3 => ECO:0000255 |
| Chain | Residue | Details |
| A | LEU175-VAL195 | |
| B | LEU175-VAL195 | |
| C | LEU175-VAL195 | |
| D | LEU175-VAL195 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S4 => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN200-ILE220 | |
| B | ASN200-ILE220 | |
| C | ASN200-ILE220 | |
| D | ASN200-ILE220 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S5 => ECO:0000255 |
| Chain | Residue | Details |
| A | VAL236-VAL256 | |
| B | VAL236-VAL256 | |
| C | VAL236-VAL256 | |
| D | VAL236-VAL256 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 88 |
| Details | INTRAMEM: Pore-forming; Name=P region => ECO:0000255 |
| Chain | Residue | Details |
| A | ALA271-VAL293 | |
| B | ALA271-VAL293 | |
| C | ALA271-VAL293 | |
| D | ALA271-VAL293 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S6 => ECO:0000255 |
| Chain | Residue | Details |
| A | PHE303-ILE323 | |
| B | PHE303-ILE323 | |
| C | PHE303-ILE323 | |
| D | PHE303-ILE323 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | GLU374 | |
| D | GLU374 | |
| D | GLN397 | |
| D | GLU399 | |
| A | GLN397 | |
| A | GLU399 | |
| B | GLU374 | |
| B | GLN397 | |
| B | GLU399 | |
| C | GLU374 | |
| C | GLN397 | |
| C | GLU399 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:B7ZC96 |
| Chain | Residue | Details |
| A | GLN947 | |
| C | ASP950 | |
| C | ASP953 | |
| C | ASP955 | |
| D | GLN947 | |
| D | ASP950 | |
| D | ASP953 | |
| D | ASP955 | |
| A | ASP950 | |
| A | ASP953 | |
| A | ASP955 | |
| B | GLN947 | |
| B | ASP950 | |
| B | ASP953 | |
| B | ASP955 | |
| C | GLN947 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q08460 |
| Chain | Residue | Details |
| A | THR698 | |
| A | THR905 | |
| B | THR698 | |
| B | THR905 | |
| C | THR698 | |
| C | THR905 | |
| D | THR698 | |
| D | THR905 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 20 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q08460 |
| Chain | Residue | Details |
| A | SER700 | |
| B | SER917 | |
| C | SER700 | |
| C | SER713 | |
| C | SER717 | |
| C | SER913 | |
| C | SER917 | |
| D | SER700 | |
| D | SER713 | |
| D | SER717 | |
| D | SER913 | |
| A | SER713 | |
| D | SER917 | |
| A | SER717 | |
| A | SER913 | |
| A | SER917 | |
| B | SER700 | |
| B | SER713 | |
| B | SER717 | |
| B | SER913 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 12 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:20693285, ECO:0000269|PubMed:22399288 |
| Chain | Residue | Details |
| A | CYS53 | |
| D | CYS53 | |
| D | CYS54 | |
| D | CYS56 | |
| A | CYS54 | |
| A | CYS56 | |
| B | CYS53 | |
| B | CYS54 | |
| B | CYS56 | |
| C | CYS53 | |
| C | CYS54 | |
| C | CYS56 |
