8B23
Time-resolved structure of K+-dependent Na+-PPase from Thermotoga maritima 600-seconds post reaction initiation with Na+
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004427 | molecular_function | inorganic diphosphate phosphatase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0006814 | biological_process | sodium ion transport |
A | 0009678 | molecular_function | diphosphate hydrolysis-driven proton transmembrane transporter activity |
A | 0015081 | molecular_function | sodium ion transmembrane transporter activity |
A | 0016020 | cellular_component | membrane |
A | 0030955 | molecular_function | potassium ion binding |
A | 0035725 | biological_process | sodium ion transmembrane transport |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 1902600 | biological_process | proton transmembrane transport |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004427 | molecular_function | inorganic diphosphate phosphatase activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005886 | cellular_component | plasma membrane |
B | 0006814 | biological_process | sodium ion transport |
B | 0009678 | molecular_function | diphosphate hydrolysis-driven proton transmembrane transporter activity |
B | 0015081 | molecular_function | sodium ion transmembrane transporter activity |
B | 0016020 | cellular_component | membrane |
B | 0030955 | molecular_function | potassium ion binding |
B | 0035725 | biological_process | sodium ion transmembrane transport |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 1902600 | biological_process | proton transmembrane transport |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 800 |
Details | TRANSMEM: Helical |
Chain | Residue | Details |
A | TYR2-PHE22 | |
A | ILE406-PHE430 | |
A | LEU437-ILE463 | |
A | THR493-SER520 | |
A | ALA542-MET571 | |
A | ILE602-LEU629 | |
A | ALA631-ALA658 | |
A | VAL698-HIS722 | |
B | TYR2-PHE22 | |
B | ASP47-PHE71 | |
B | TRP74-MET97 | |
A | ASP47-PHE71 | |
B | TYR123-GLY153 | |
B | PHE169-TYR197 | |
B | ASP236-TYR261 | |
B | ALA285-ILE309 | |
B | LEU321-TYR343 | |
B | ALA359-TRP379 | |
B | ILE406-PHE430 | |
B | LEU437-ILE463 | |
B | THR493-SER520 | |
B | ALA542-MET571 | |
A | TRP74-MET97 | |
B | ILE602-LEU629 | |
B | ALA631-ALA658 | |
B | VAL698-HIS722 | |
A | TYR123-GLY153 | |
A | PHE169-TYR197 | |
A | ASP236-TYR261 | |
A | ALA285-ILE309 | |
A | LEU321-TYR343 | |
A | ALA359-TRP379 |
site_id | SWS_FT_FI2 |
Number of Residues | 428 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:22837527 |
Chain | Residue | Details |
A | ALA23-ALA46 | |
B | ALA98-ALA122 | |
B | THR198-GLY235 | |
B | VAL310-GLU320 | |
B | ALA380-VAL405 | |
B | ALA464-ASN492 | |
B | LYS572-GLU601 | |
B | TRP659-THR697 | |
A | ALA98-ALA122 | |
A | THR198-GLY235 | |
A | VAL310-GLU320 | |
A | ALA380-VAL405 | |
A | ALA464-ASN492 | |
A | LYS572-GLU601 | |
A | TRP659-THR697 | |
B | ALA23-ALA46 |
site_id | SWS_FT_FI3 |
Number of Residues | 160 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:22837527 |
Chain | Residue | Details |
A | THR72-THR73 | |
B | GLN154-ASN168 | |
B | MET262-GLN284 | |
B | LEU344-GLY358 | |
B | ALA431-GLY436 | |
B | GLN521-ASP541 | |
B | GLY630 | |
B | VAL723-PHE726 | |
A | GLN154-ASN168 | |
A | MET262-GLN284 | |
A | LEU344-GLY358 | |
A | ALA431-GLY436 | |
A | GLN521-ASP541 | |
A | GLY630 | |
A | VAL723-PHE726 | |
B | THR72-THR73 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS199 | |
A | LYS695 | |
B | LYS199 | |
B | LYS695 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP202 | |
A | ASP206 | |
B | ASP202 | |
B | ASP206 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22837527 |
Chain | Residue | Details |
A | ASN229 | |
A | ASP232 | |
A | ASP465 | |
B | ASN229 | |
B | ASP232 | |
B | ASP465 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22837527, ECO:0007744|PDB:4AV3 |
Chain | Residue | Details |
A | ASP660 | |
A | ASP688 | |
A | ASP692 | |
B | ASP660 | |
B | ASP688 | |
B | ASP692 |
site_id | SWS_FT_FI8 |
Number of Residues | 10 |
Details | SITE: Important for ion transport => ECO:0000250 |
Chain | Residue | Details |
A | ARG191 | |
B | LYS707 | |
A | ASP236 | |
A | ASP243 | |
A | ASP696 | |
A | LYS707 | |
B | ARG191 | |
B | ASP236 | |
B | ASP243 | |
B | ASP696 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | SITE: Determinant of potassium dependence => ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000305 |
Chain | Residue | Details |
A | ALA495 | |
B | ALA495 |