6QXA
Structure of membrane bound pyrophosphatase from Thermotoga maritima in complex with imidodiphosphate and N-[(2-amino-6-benzothiazolyl)methyl]-1H-indole-2-carboxamide (ATC)
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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004427 | molecular_function | inorganic diphosphate phosphatase activity |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006814 | biological_process | sodium ion transport |
| C | 0009678 | molecular_function | diphosphate hydrolysis-driven proton transmembrane transporter activity |
| C | 0015081 | molecular_function | sodium ion transmembrane transporter activity |
| C | 0016020 | cellular_component | membrane |
| C | 0030955 | molecular_function | potassium ion binding |
| C | 0035725 | biological_process | sodium ion transmembrane transport |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1902600 | biological_process | proton transmembrane transport |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004427 | molecular_function | inorganic diphosphate phosphatase activity |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006814 | biological_process | sodium ion transport |
| D | 0009678 | molecular_function | diphosphate hydrolysis-driven proton transmembrane transporter activity |
| D | 0015081 | molecular_function | sodium ion transmembrane transporter activity |
| D | 0016020 | cellular_component | membrane |
| D | 0030955 | molecular_function | potassium ion binding |
| D | 0035725 | biological_process | sodium ion transmembrane transport |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 801 |
| Chain | Residue |
| A | ASP202 |
| A | ASP206 |
| A | MG803 |
| A | 2PN806 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 802 |
| Chain | Residue |
| A | ASP218 |
| A | ASP465 |
| A | 2PN806 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 803 |
| Chain | Residue |
| A | MG801 |
| A | 2PN806 |
| A | ASP202 |
| A | ASP692 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 804 |
| Chain | Residue |
| A | ASP228 |
| 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 | 17 |
| Details | binding site for residue 2PN A 806 |
| Chain | Residue |
| A | LYS199 |
| A | ASP202 |
| A | GLU217 |
| A | ASP232 |
| A | ASP465 |
| A | ASP488 |
| A | ASP660 |
| A | LYS664 |
| A | ASP692 |
| A | LYS695 |
| A | ASP696 |
| A | MG801 |
| A | MG802 |
| A | MG803 |
| A | MG804 |
| A | MG805 |
| A | K808 |
| 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 K A 808 |
| Chain | Residue |
| A | 2PN806 |
| A | HOH901 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue GQB A 809 |
| Chain | Residue |
| A | GLN268 |
| A | GLN277 |
| A | GLY528 |
| A | PRO530 |
| A | GQB810 |
| D | ILE70 |
| D | THR72 |
| D | THR73 |
| D | TRP74 |
| D | TRP164 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue GQB A 810 |
| Chain | Residue |
| A | GLN268 |
| A | GLN277 |
| A | ASP351 |
| A | VAL352 |
| A | GQB809 |
| D | TRP74 |
| D | ASN157 |
| D | TYR161 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 801 |
| Chain | Residue |
| B | LYS199 |
| B | ASP202 |
| B | ASP688 |
| B | ASP692 |
| B | MG805 |
| B | 2PN806 |
| site_id | AD3 |
| 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 | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 803 |
| Chain | Residue |
| B | ASP232 |
| B | ASP465 |
| B | MG802 |
| B | 2PN806 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 804 |
| Chain | Residue |
| B | ASP488 |
| B | ASN492 |
| B | ASP660 |
| B | 2PN806 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 805 |
| Chain | Residue |
| B | ASP202 |
| B | ASP206 |
| B | ASP688 |
| B | MG801 |
| B | 2PN806 |
| site_id | AD7 |
| Number of Residues | 16 |
| Details | binding site for residue 2PN B 806 |
| Chain | Residue |
| B | MG805 |
| B | K808 |
| B | LYS199 |
| B | ASP202 |
| B | GLU217 |
| B | ASP228 |
| B | ASP232 |
| B | ASP465 |
| B | ASN492 |
| B | ASP688 |
| B | ASP692 |
| B | LYS695 |
| B | MG801 |
| B | MG802 |
| B | MG803 |
| B | MG804 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 807 |
| Chain | Residue |
| B | ASP243 |
| B | GLU246 |
| B | SER247 |
| B | ASP703 |
| B | LYS707 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue K B 808 |
| Chain | Residue |
| B | ASP236 |
| B | 2PN806 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 801 |
| Chain | Residue |
| C | ASP202 |
| C | ASP206 |
| C | ASP688 |
| C | MG803 |
| C | 2PN806 |
| C | HOH903 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 802 |
| Chain | Residue |
| C | ASP228 |
| C | ASP232 |
| C | ASP465 |
| C | MG804 |
| C | 2PN806 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 803 |
| Chain | Residue |
| C | ASP202 |
| C | ASP688 |
| C | ASP692 |
| C | MG801 |
| C | 2PN806 |
| site_id | AE4 |
| Number of Residues | 7 |
| Details | binding site for residue MG C 804 |
| Chain | Residue |
| C | ASP218 |
| C | ASP228 |
| C | ASP232 |
| C | ASP465 |
| C | MG802 |
| C | 2PN806 |
| C | HOH901 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 805 |
| Chain | Residue |
| C | ASP488 |
| C | ASN492 |
| C | ASP660 |
| C | 2PN806 |
| site_id | AE6 |
| Number of Residues | 16 |
| Details | binding site for residue 2PN C 806 |
| Chain | Residue |
| C | LYS199 |
| C | ASP202 |
| C | GLU217 |
| C | ASP232 |
| C | ASP236 |
| C | ASP465 |
| C | ASN492 |
| C | ASP692 |
| C | LYS695 |
| C | ASP696 |
| C | MG801 |
| C | MG802 |
| C | MG803 |
| C | MG804 |
| C | MG805 |
| C | HOH903 |
| site_id | AE7 |
| Number of Residues | 3 |
| Details | binding site for residue D1D C 807 |
| Chain | Residue |
| A | ASN597 |
| A | ILE600 |
| C | ASN597 |
| site_id | AE8 |
| Number of Residues | 7 |
| Details | binding site for residue GQB C 808 |
| Chain | Residue |
| B | MET69 |
| B | ILE70 |
| B | THR72 |
| B | TRP164 |
| C | GLN268 |
| C | LYS269 |
| C | GLY528 |
| site_id | AE9 |
| Number of Residues | 3 |
| Details | binding site for residue MG D 801 |
| Chain | Residue |
| D | ASP202 |
| D | ASP206 |
| D | 2PN806 |
| site_id | AF1 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 802 |
| Chain | Residue |
| D | ASP218 |
| D | ASP228 |
| D | ASN229 |
| D | ASP232 |
| D | ASP465 |
| D | 2PN806 |
| site_id | AF2 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 803 |
| Chain | Residue |
| D | ASP232 |
| D | ASP465 |
| D | 2PN806 |
| D | K808 |
| site_id | AF3 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 804 |
| Chain | Residue |
| D | ASP488 |
| D | ASN492 |
| D | ASP660 |
| D | 2PN806 |
| site_id | AF4 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 805 |
| Chain | Residue |
| D | ASP660 |
| D | ASP688 |
| D | ASP692 |
| D | LYS695 |
| D | 2PN806 |
| site_id | AF5 |
| Number of Residues | 20 |
| Details | binding site for residue 2PN D 806 |
| Chain | Residue |
| D | LYS199 |
| D | ASP202 |
| D | ASP206 |
| D | GLU217 |
| D | ASP228 |
| D | ASP232 |
| D | ASP465 |
| D | ASP488 |
| D | ASN492 |
| D | ASP660 |
| D | LYS663 |
| D | ASP692 |
| D | LYS695 |
| D | MG801 |
| D | MG802 |
| D | MG803 |
| D | MG804 |
| D | MG805 |
| D | K808 |
| D | HOH902 |
| site_id | AF6 |
| Number of Residues | 5 |
| Details | binding site for residue NA D 807 |
| Chain | Residue |
| D | ASP243 |
| D | SER247 |
| D | ALA502 |
| D | ASP703 |
| D | LYS707 |
| site_id | AF7 |
| Number of Residues | 5 |
| Details | binding site for residue K D 808 |
| Chain | Residue |
| D | ASP236 |
| D | ASN492 |
| D | LYS695 |
| D | MG803 |
| D | 2PN806 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1600 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| A | TYR2-PHE22 | |
| A | ASP47-PHE71 | |
| A | TRP74-MET97 | |
| A | TYR123-GLY153 | |
| A | PHE169-TYR197 | |
| A | ASP236-TYR261 | |
| A | ALA285-ILE309 | |
| A | LEU321-TYR343 | |
| A | ALA359-TRP379 | |
| 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 | |
| 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 | |
| B | ILE602-LEU629 | |
| B | ALA631-ALA658 | |
| B | VAL698-HIS722 | |
| C | TYR2-PHE22 | |
| C | ASP47-PHE71 | |
| C | TRP74-MET97 | |
| C | TYR123-GLY153 | |
| C | PHE169-TYR197 | |
| C | ASP236-TYR261 | |
| C | ALA285-ILE309 | |
| C | LEU321-TYR343 | |
| C | ALA359-TRP379 | |
| C | ILE406-PHE430 | |
| C | LEU437-ILE463 | |
| C | THR493-SER520 | |
| C | ALA542-MET571 | |
| C | ILE602-LEU629 | |
| C | ALA631-ALA658 | |
| C | VAL698-HIS722 | |
| D | TYR2-PHE22 | |
| D | ASP47-PHE71 | |
| D | TRP74-MET97 | |
| D | TYR123-GLY153 | |
| D | PHE169-TYR197 | |
| D | ASP236-TYR261 | |
| D | ALA285-ILE309 | |
| D | LEU321-TYR343 | |
| D | ALA359-TRP379 | |
| D | ILE406-PHE430 | |
| D | LEU437-ILE463 | |
| D | THR493-SER520 | |
| D | ALA542-MET571 | |
| D | ILE602-LEU629 | |
| D | ALA631-ALA658 | |
| D | VAL698-HIS722 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 856 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:22837527 |
| Chain | Residue | Details |
| A | ALA23-ALA46 | |
| A | ALA98-ALA122 | |
| A | THR198-GLY235 | |
| A | VAL310-GLU320 | |
| A | ALA380-VAL405 | |
| A | ALA464-ASN492 | |
| A | LYS572-GLU601 | |
| A | TRP659-THR697 | |
| B | ALA23-ALA46 | |
| B | ALA98-ALA122 | |
| B | THR198-GLY235 | |
| B | VAL310-GLU320 | |
| B | ALA380-VAL405 | |
| B | ALA464-ASN492 | |
| B | LYS572-GLU601 | |
| B | TRP659-THR697 | |
| C | ALA23-ALA46 | |
| C | ALA98-ALA122 | |
| C | THR198-GLY235 | |
| C | VAL310-GLU320 | |
| C | ALA380-VAL405 | |
| C | ALA464-ASN492 | |
| C | LYS572-GLU601 | |
| C | TRP659-THR697 | |
| D | ALA23-ALA46 | |
| D | ALA98-ALA122 | |
| D | THR198-GLY235 | |
| D | VAL310-GLU320 | |
| D | ALA380-VAL405 | |
| D | ALA464-ASN492 | |
| D | LYS572-GLU601 | |
| D | TRP659-THR697 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 320 |
| Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:22837527 |
| Chain | Residue | Details |
| A | THR72-THR73 | |
| A | GLN154-ASN168 | |
| A | MET262-GLN284 | |
| A | LEU344-GLY358 | |
| A | ALA431-GLY436 | |
| A | GLN521-ASP541 | |
| A | VAL723-PHE726 | |
| B | THR72-THR73 | |
| B | GLN154-ASN168 | |
| B | MET262-GLN284 | |
| B | LEU344-GLY358 | |
| B | ALA431-GLY436 | |
| B | GLN521-ASP541 | |
| B | VAL723-PHE726 | |
| C | THR72-THR73 | |
| C | GLN154-ASN168 | |
| C | MET262-GLN284 | |
| C | LEU344-GLY358 | |
| C | ALA431-GLY436 | |
| C | GLN521-ASP541 | |
| C | VAL723-PHE726 | |
| D | THR72-THR73 | |
| D | GLN154-ASN168 | |
| D | MET262-GLN284 | |
| D | LEU344-GLY358 | |
| D | ALA431-GLY436 | |
| D | GLN521-ASP541 | |
| D | VAL723-PHE726 | |
| A | GLY630 | |
| B | GLY630 | |
| C | GLY630 | |
| D | GLY630 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS199 | |
| A | LYS695 | |
| B | LYS199 | |
| B | LYS695 | |
| C | LYS199 | |
| C | LYS695 | |
| D | LYS199 | |
| D | LYS695 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP202 | |
| A | ASP206 | |
| B | ASP202 | |
| B | ASP206 | |
| C | ASP202 | |
| C | ASP206 | |
| D | ASP202 | |
| D | ASP206 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22837527 |
| Chain | Residue | Details |
| A | ASN229 | |
| A | ASP232 | |
| A | ASP465 | |
| B | ASN229 | |
| B | ASP232 | |
| B | ASP465 | |
| C | ASN229 | |
| C | ASP232 | |
| C | ASP465 | |
| D | ASN229 | |
| D | ASP232 | |
| D | ASP465 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22837527, ECO:0007744|PDB:4AV3 |
| Chain | Residue | Details |
| C | ASP692 | |
| D | ASP660 | |
| D | ASP688 | |
| D | ASP692 | |
| A | ASP660 | |
| A | ASP688 | |
| A | ASP692 | |
| B | ASP660 | |
| B | ASP688 | |
| B | ASP692 | |
| C | ASP660 | |
| C | ASP688 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | SITE: Important for ion transport => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG191 | |
| A | ASP236 | |
| A | ASP243 | |
| A | ASP696 | |
| A | LYS707 | |
| B | ARG191 | |
| B | ASP236 | |
| B | ASP243 | |
| B | ASP696 | |
| B | LYS707 | |
| C | ARG191 | |
| C | ASP236 | |
| C | ASP243 | |
| C | ASP696 | |
| C | LYS707 | |
| D | ARG191 | |
| D | ASP236 | |
| D | ASP243 | |
| D | ASP696 | |
| D | LYS707 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | SITE: Determinant of potassium dependence => ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000305 |
| Chain | Residue | Details |
| A | ALA495 | |
| B | ALA495 | |
| C | ALA495 | |
| D | ALA495 |
