3EFF
The Crystal Structure of Full-Length KcsA in its Closed Conformation
Functional Information from GO Data
Chain | GOid | namespace | contents |
K | 0005249 | molecular_function | voltage-gated potassium channel activity |
K | 0006813 | biological_process | potassium ion transport |
K | 0008076 | cellular_component | voltage-gated potassium channel complex |
L | 0005249 | molecular_function | voltage-gated potassium channel activity |
L | 0006813 | biological_process | potassium ion transport |
L | 0008076 | cellular_component | voltage-gated potassium channel complex |
M | 0005249 | molecular_function | voltage-gated potassium channel activity |
M | 0006813 | biological_process | potassium ion transport |
M | 0008076 | cellular_component | voltage-gated potassium channel complex |
N | 0005249 | molecular_function | voltage-gated potassium channel activity |
N | 0006813 | biological_process | potassium ion transport |
N | 0008076 | cellular_component | voltage-gated potassium channel complex |
Functional Information from PROSITE/UniProt
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH |
Chain | Residue | Details |
A | TYR194-HIS200 | |
B | TYR205-HIS211 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 180 |
Details | Transmembrane: {"description":"Helical"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 64 |
Details | Topological domain: {"description":"Extracellular"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | Intramembrane: {"description":"Helical; Pore-forming"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 28 |
Details | Intramembrane: {"description":"Pore-forming"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 192 |
Details | Topological domain: {"description":"Cytoplasmic"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | Motif: {"description":"Selectivity filter"} |
Chain | Residue | Details |