7ZRM
Cryo-EM map of the unphosphorylated KdpFABC complex in the E1-P_ADP conformation, under turnover conditions
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006813 | biological_process | potassium ion transport |
| A | 0008556 | molecular_function | P-type potassium transmembrane transporter activity |
| A | 0016020 | cellular_component | membrane |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0031004 | cellular_component | potassium ion-transporting ATPase complex |
| A | 0071805 | biological_process | potassium ion transmembrane transport |
| A | 0098655 | biological_process | monoatomic cation transmembrane transport |
| A | 1903103 | cellular_component | potassium:proton antiporter complex |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005215 | molecular_function | transporter activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0006813 | biological_process | potassium ion transport |
| B | 0008556 | molecular_function | P-type potassium transmembrane transporter activity |
| B | 0015662 | molecular_function | P-type ion transporter activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0031004 | cellular_component | potassium ion-transporting ATPase complex |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071805 | biological_process | potassium ion transmembrane transport |
| B | 0098655 | biological_process | monoatomic cation transmembrane transport |
| B | 1903103 | cellular_component | potassium:proton antiporter complex |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006811 | biological_process | monoatomic ion transport |
| C | 0006813 | biological_process | potassium ion transport |
| C | 0008556 | molecular_function | P-type potassium transmembrane transporter activity |
| C | 0016020 | cellular_component | membrane |
| C | 0031004 | cellular_component | potassium ion-transporting ATPase complex |
| C | 0071805 | biological_process | potassium ion transmembrane transport |
| C | 0098655 | biological_process | monoatomic cation transmembrane transport |
| C | 1903103 | cellular_component | potassium:proton antiporter complex |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006811 | biological_process | monoatomic ion transport |
| D | 0006813 | biological_process | potassium ion transport |
| D | 0008556 | molecular_function | P-type potassium transmembrane transporter activity |
| D | 0016020 | cellular_component | membrane |
| D | 0031004 | cellular_component | potassium ion-transporting ATPase complex |
| D | 0043462 | biological_process | regulation of ATP-dependent activity |
| D | 0071805 | biological_process | potassium ion transmembrane transport |
| D | 0098655 | biological_process | monoatomic cation transmembrane transport |
| D | 1903103 | cellular_component | potassium:proton antiporter complex |
Functional Information from PROSITE/UniProt
| site_id | PS00154 |
| Number of Residues | 7 |
| Details | ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTIT |
| Chain | Residue | Details |
| B | PHD307-THR313 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 199 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"28636601","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7896809","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 344 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"28636601","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MRW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 124 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28636601","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7896809","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28636601","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30478378","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 49 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"28636601","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30478378","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MRW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HRA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 156 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"28636601","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30478378","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 29 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"28636601","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 162 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28636601","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Active site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_00285","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474895","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00285","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16354672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A00","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A29","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00285","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16354672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A00","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00285","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"28636601","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30478378","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
