3PJZ
Crystal Structure of the Potassium Transporter TrkH from Vibrio parahaemolyticus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005267 | molecular_function | potassium channel activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0006812 | biological_process | monoatomic cation transport |
A | 0006813 | biological_process | potassium ion transport |
A | 0008324 | molecular_function | monoatomic cation transmembrane transporter activity |
A | 0015379 | molecular_function | potassium:chloride symporter activity |
A | 0016020 | cellular_component | membrane |
A | 0030001 | biological_process | metal ion transport |
A | 0030955 | molecular_function | potassium ion binding |
A | 0034220 | biological_process | monoatomic ion transmembrane transport |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0055085 | biological_process | transmembrane transport |
A | 0071805 | biological_process | potassium ion transmembrane transport |
B | 0005267 | molecular_function | potassium channel activity |
B | 0005886 | cellular_component | plasma membrane |
B | 0006812 | biological_process | monoatomic cation transport |
B | 0006813 | biological_process | potassium ion transport |
B | 0008324 | molecular_function | monoatomic cation transmembrane transporter activity |
B | 0015379 | molecular_function | potassium:chloride symporter activity |
B | 0016020 | cellular_component | membrane |
B | 0030001 | biological_process | metal ion transport |
B | 0030955 | molecular_function | potassium ion binding |
B | 0034220 | biological_process | monoatomic ion transmembrane transport |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0055085 | biological_process | transmembrane transport |
B | 0071805 | biological_process | potassium ion transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE K A 501 |
Chain | Residue |
A | THR111 |
A | THR112 |
A | ILE220 |
A | GLY221 |
A | THR320 |
A | ALA321 |
A | ASN437 |
A | LEU438 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE K B 501 |
Chain | Residue |
B | THR112 |
B | ILE220 |
B | GLY221 |
B | THR320 |
B | ALA321 |
B | ASN437 |
B | LEU438 |
B | THR111 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 68 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:21317882 |
Chain | Residue | Details |
A | MET1-GLN2 | |
A | ARG58-LYS65 | |
A | PRO151-ARG177 | |
B | MET1-GLN2 | |
B | ARG58-LYS65 | |
B | PRO151-ARG177 |
site_id | SWS_FT_FI2 |
Number of Residues | 334 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:21317882 |
Chain | Residue | Details |
A | PHE3-LEU29 | |
B | SER66-ILE90 | |
B | LYS125-LEU150 | |
B | ILE178-LEU202 | |
B | PHE276-LYS296 | |
B | PRO392-ALA419 | |
A | GLY36-ASN57 | |
A | SER66-ILE90 | |
A | LYS125-LEU150 | |
A | ILE178-LEU202 | |
A | PHE276-LYS296 | |
A | PRO392-ALA419 | |
B | PHE3-LEU29 | |
B | GLY36-ASN57 |
site_id | SWS_FT_FI3 |
Number of Residues | 90 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:21317882 |
Chain | Residue | Details |
A | LEU30-ALA35 | |
B | LEU30-ALA35 | |
B | ALA91 | |
B | VAL116-PRO124 | |
B | ALA203-MET205 | |
B | THR225-ASP234 | |
B | HIS297 | |
B | THR325-PRO332 | |
B | THR420-GLY421 | |
B | LEU442-ASN453 | |
A | ALA91 | |
A | VAL116-PRO124 | |
A | ALA203-MET205 | |
A | THR225-ASP234 | |
A | HIS297 | |
A | THR325-PRO332 | |
A | THR420-GLY421 | |
A | LEU442-ASN453 |
site_id | SWS_FT_FI4 |
Number of Residues | 94 |
Details | INTRAMEM: Helical; Pore-forming => ECO:0000269|PubMed:21317882 |
Chain | Residue | Details |
A | VAL98-LEU109 | |
A | PRO207-ILE218 | |
A | PRO303-SER318 | |
A | GLU424-THR434 | |
B | VAL98-LEU109 | |
B | PRO207-ILE218 | |
B | PRO303-SER318 | |
B | GLU424-THR434 |
site_id | SWS_FT_FI5 |
Number of Residues | 50 |
Details | INTRAMEM: INTRAMEM => ECO:0000269|PubMed:21317882 |
Chain | Residue | Details |
A | THR110-THR115 | |
B | THR206 | |
B | ALA219-SER224 | |
B | CYS251 | |
B | THR319-THR324 | |
B | MET422-ASP423 | |
B | LEU435-GLY441 | |
B | PHE466 | |
A | THR206 | |
A | ALA219-SER224 | |
A | CYS251 | |
A | THR319-THR324 | |
A | MET422-ASP423 | |
A | LEU435-GLY441 | |
A | PHE466 | |
B | THR110-THR115 |
site_id | SWS_FT_FI6 |
Number of Residues | 76 |
Details | INTRAMEM: Helical => ECO:0000269|PubMed:21317882 |
Chain | Residue | Details |
A | SER235-ALA250 | |
A | LEU333-PHE344 | |
A | VAL358 | |
A | ASP454-LEU465 | |
B | SER235-ALA250 | |
B | LEU333-PHE344 | |
B | VAL358 | |
B | ASP454-LEU465 |
site_id | SWS_FT_FI7 |
Number of Residues | 24 |
Details | INTRAMEM: Note=Loop between two helices => ECO:0000269|PubMed:21317882 |
Chain | Residue | Details |
A | ILE345-LYS357 | |
B | ILE345-LYS357 |
site_id | SWS_FT_FI8 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21317882 |
Chain | Residue | Details |
A | THR111 | |
B | THR112 | |
B | ILE220 | |
B | GLY221 | |
B | THR320 | |
B | ALA321 | |
B | ASN437 | |
B | LEU438 | |
A | THR112 | |
A | ILE220 | |
A | GLY221 | |
A | THR320 | |
A | ALA321 | |
A | ASN437 | |
A | LEU438 | |
B | THR111 |