5LZQ
Crystal structure of Thermotoga maritima sodium pumping membrane integral pyrophosphatase in complex with imidodiphosphate and magnesium, and with bound sodium ion
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 | 0006811 | biological_process | monoatomic ion transport |
| 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 | 0006811 | biological_process | monoatomic ion transport |
| 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 PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 801 |
| Chain | Residue |
| A | ASP202 |
| A | ASP206 |
| A | ASP688 |
| A | MG803 |
| A | 2PN806 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 802 |
| Chain | Residue |
| A | ASP218 |
| A | ASP228 |
| A | ASP465 |
| A | 2PN806 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 803 |
| Chain | Residue |
| A | ASP202 |
| A | ASP688 |
| A | ASP692 |
| A | MG801 |
| A | 2PN806 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 804 |
| Chain | Residue |
| A | ASP232 |
| A | ASP465 |
| A | 2PN806 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 805 |
| Chain | Residue |
| A | ASP488 |
| A | ASN492 |
| A | ASP660 |
| A | 2PN806 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue 2PN A 806 |
| Chain | Residue |
| A | LYS199 |
| A | ASP202 |
| A | GLU217 |
| A | ASP232 |
| A | ASP236 |
| A | ASP465 |
| A | ASP488 |
| A | ASN492 |
| A | ASP660 |
| A | ASP692 |
| A | MG801 |
| A | MG802 |
| A | MG803 |
| A | MG804 |
| A | MG805 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 807 |
| Chain | Residue |
| A | ASP243 |
| A | GLU246 |
| A | SER247 |
| A | ASP703 |
| A | LYS707 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue 2PN A 808 |
| Chain | Residue |
| A | LYS269 |
| A | GLU272 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue 2PN A 809 |
| Chain | Residue |
| A | MET518 |
| A | LEU533 |
| A | VAL534 |
| A | LEU536 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 801 |
| Chain | Residue |
| B | ASP202 |
| B | ASP688 |
| B | ASP692 |
| B | MG805 |
| B | 2PN806 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 802 |
| Chain | Residue |
| B | ASP218 |
| B | ASP228 |
| B | ASP465 |
| B | MG803 |
| B | 2PN806 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 803 |
| Chain | Residue |
| B | ASP228 |
| B | ASP232 |
| B | ASP465 |
| B | MG802 |
| B | 2PN806 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 804 |
| Chain | Residue |
| B | ASP488 |
| B | ASN492 |
| B | ASP660 |
| B | 2PN806 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 805 |
| Chain | Residue |
| B | ASP202 |
| B | ASP206 |
| B | MG801 |
| B | 2PN806 |
| site_id | AD6 |
| Number of Residues | 14 |
| Details | binding site for residue 2PN B 806 |
| Chain | Residue |
| B | ASP202 |
| B | GLU217 |
| B | ASP465 |
| B | ASP488 |
| B | ASN492 |
| B | ASP660 |
| B | LYS663 |
| B | ASP692 |
| B | LYS695 |
| B | MG801 |
| B | MG802 |
| B | MG803 |
| B | MG804 |
| B | MG805 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 807 |
| Chain | Residue |
| B | ASP243 |
| B | GLU246 |
| B | SER247 |
| B | ASP703 |
| B | LYS707 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 800 |
| Details | Transmembrane: {"description":"Helical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 428 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"22837527","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 160 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"22837527","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22837527","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22837527","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AV3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 10 |
| Details | Site: {"description":"Important for ion transport","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Site: {"description":"Determinant of potassium dependence","evidences":[{"source":"HAMAP-Rule","id":"MF_01129","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
