5YLU
Crystal structure of the gastric proton pump complexed with vonoprazan
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005215 | molecular_function | transporter activity |
| A | 0005391 | molecular_function | P-type sodium:potassium-exchanging transporter activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005889 | cellular_component | potassium:proton exchanging ATPase complex |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006813 | biological_process | potassium ion transport |
| A | 0006883 | biological_process | intracellular sodium ion homeostasis |
| A | 0008556 | molecular_function | P-type potassium transmembrane transporter activity |
| A | 0008900 | molecular_function | P-type potassium:proton transporter activity |
| A | 0010248 | biological_process | establishment or maintenance of transmembrane electrochemical gradient |
| A | 0016020 | cellular_component | membrane |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0030007 | biological_process | intracellular potassium ion homeostasis |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0036376 | biological_process | sodium ion export across plasma membrane |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071805 | biological_process | potassium ion transmembrane transport |
| A | 0090533 | cellular_component | cation-transporting ATPase complex |
| A | 0098797 | cellular_component | plasma membrane protein complex |
| A | 1902600 | biological_process | proton transmembrane transport |
| A | 1990573 | biological_process | potassium ion import across plasma membrane |
| B | 0001671 | molecular_function | ATPase activator activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005889 | cellular_component | potassium:proton exchanging ATPase complex |
| B | 0005890 | cellular_component | sodium:potassium-exchanging ATPase complex |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0006813 | biological_process | potassium ion transport |
| B | 0006814 | biological_process | sodium ion transport |
| B | 0006883 | biological_process | intracellular sodium ion homeostasis |
| B | 0007155 | biological_process | cell adhesion |
| B | 0016020 | cellular_component | membrane |
| B | 0016324 | cellular_component | apical plasma membrane |
| B | 0030007 | biological_process | intracellular potassium ion homeostasis |
| B | 0036376 | biological_process | sodium ion export across plasma membrane |
| B | 0071805 | biological_process | potassium ion transmembrane transport |
| B | 1902600 | biological_process | proton transmembrane transport |
| B | 1990573 | biological_process | potassium ion import across plasma membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00154 |
| Number of Residues | 7 |
| Details | ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT |
| Chain | Residue | Details |
| A | BFD385-THR391 |
| site_id | PS00390 |
| Number of Residues | 21 |
| Details | ATPASE_NA_K_BETA_1 Sodium and potassium ATPases beta subunits signature 1. FqrYcWNpdtgqmLGRTlsrW |
| Chain | Residue | Details |
| B | PHE17-TRP37 |
| site_id | PS00391 |
| Number of Residues | 16 |
| Details | ATPASE_NA_K_BETA_2 Sodium and potassium ATPases beta subunits signature 2. KfsCKftadmLqnCSG |
| Chain | Residue | Details |
| B | LYS149-GLY164 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 194 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 107 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 167 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 22 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Active site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"PubMed","id":"1720615","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31436534","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6JXH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29618813","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31436534","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5YLU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6JXH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q6PIE5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50993","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09626","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 232 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 96 |
| Details | Region: {"description":"immunoglobulin-like","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"UniProtKB","id":"P18597","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
