4AV6
Crystal structure of Thermotoga maritima sodium pumping membrane integral pyrophosphatase at 4 A in complex with phosphate and magnesium
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 PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1727 |
| Chain | Residue |
| A | ASP202 |
| A | MG1731 |
| A | MG1732 |
| A | ASP232 |
| A | ASP465 |
| A | ASP488 |
| A | ASP660 |
| A | LYS664 |
| A | PO41728 |
| A | MG1729 |
| A | MG1730 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1728 |
| Chain | Residue |
| A | LYS199 |
| A | ASP236 |
| A | ASN492 |
| A | ASP660 |
| A | ASP692 |
| A | ASP696 |
| A | PO41727 |
| A | MG1731 |
| A | MG1732 |
| A | K1733 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1729 |
| Chain | Residue |
| A | ASP202 |
| A | ASP206 |
| A | ASP228 |
| A | PO41727 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1730 |
| Chain | Residue |
| A | ASP232 |
| A | ASP465 |
| A | PO41727 |
| A | MG1732 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 1731 |
| Chain | Residue |
| A | ASP202 |
| A | ASP660 |
| A | ASP688 |
| A | ASP692 |
| A | LYS695 |
| A | PO41727 |
| A | PO41728 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1732 |
| Chain | Residue |
| A | ASP232 |
| A | ASP465 |
| A | PO41727 |
| A | PO41728 |
| A | MG1730 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 1733 |
| Chain | Residue |
| A | ASN492 |
| A | ALA495 |
| A | ASP696 |
| A | PO41728 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1727 |
| Chain | Residue |
| B | ASP202 |
| B | ASP232 |
| B | ASP465 |
| B | ASP488 |
| B | ASP660 |
| B | LYS663 |
| B | LYS664 |
| B | PO41728 |
| B | MG1729 |
| B | MG1730 |
| B | MG1731 |
| B | MG1732 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1728 |
| Chain | Residue |
| B | LYS199 |
| B | ASP236 |
| B | ASP465 |
| B | ASN492 |
| B | ASP660 |
| B | ASP696 |
| B | PO41727 |
| B | MG1731 |
| B | MG1732 |
| B | K1733 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 1729 |
| Chain | Residue |
| B | ASP202 |
| B | ASP206 |
| B | ASP688 |
| B | PO41727 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 1730 |
| Chain | Residue |
| B | PO41727 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 1731 |
| Chain | Residue |
| B | ASP202 |
| B | ASP660 |
| B | ASP688 |
| B | ASP692 |
| B | LYS695 |
| B | PO41727 |
| B | PO41728 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 1732 |
| Chain | Residue |
| B | ASP232 |
| B | ASP465 |
| B | PO41727 |
| B | PO41728 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 1733 |
| Chain | Residue |
| B | ASN492 |
| B | ALA495 |
| B | LYS695 |
| B | ASP696 |
| B | PO41728 |
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 |
