5GPJ
Crystal Structure of Proton-Pumping Pyrophosphatase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004427 | molecular_function | inorganic diphosphate phosphatase activity |
| A | 0005773 | cellular_component | vacuole |
| A | 0005774 | cellular_component | vacuolar membrane |
| A | 0009678 | molecular_function | diphosphate hydrolysis-driven proton transmembrane transporter activity |
| A | 0016020 | cellular_component | membrane |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0004427 | molecular_function | inorganic diphosphate phosphatase activity |
| B | 0005773 | cellular_component | vacuole |
| B | 0005774 | cellular_component | vacuolar membrane |
| B | 0009678 | molecular_function | diphosphate hydrolysis-driven proton transmembrane transporter activity |
| B | 0016020 | cellular_component | membrane |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1902600 | biological_process | proton transmembrane transport |
| C | 0004427 | molecular_function | inorganic diphosphate phosphatase activity |
| C | 0005773 | cellular_component | vacuole |
| C | 0005774 | cellular_component | vacuolar membrane |
| C | 0009678 | molecular_function | diphosphate hydrolysis-driven proton transmembrane transporter activity |
| C | 0016020 | cellular_component | membrane |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1902600 | biological_process | proton transmembrane transport |
| D | 0004427 | molecular_function | inorganic diphosphate phosphatase activity |
| D | 0005773 | cellular_component | vacuole |
| D | 0005774 | cellular_component | vacuolar membrane |
| D | 0009678 | molecular_function | diphosphate hydrolysis-driven proton transmembrane transporter activity |
| D | 0016020 | cellular_component | membrane |
| 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 | 8 |
| Details | binding site for residue PO4 A 1001 |
| Chain | Residue |
| A | LYS250 |
| A | ASP253 |
| A | ASP279 |
| A | ASP283 |
| A | ASP507 |
| A | LYS730 |
| A | MG1002 |
| A | MG1003 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue MG A 1002 |
| Chain | Residue |
| A | PO41001 |
| A | ASP507 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 1003 |
| Chain | Residue |
| A | ASP253 |
| A | ASP723 |
| A | ASP727 |
| A | LYS730 |
| A | PO41001 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue PO4 B 1001 |
| Chain | Residue |
| B | LYS250 |
| B | ASP253 |
| B | ASP279 |
| B | ASP283 |
| B | ASP507 |
| B | ASP723 |
| B | LYS730 |
| B | MG1002 |
| B | MG1003 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 1002 |
| Chain | Residue |
| B | ASP507 |
| B | PO41001 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 1003 |
| Chain | Residue |
| B | ASP253 |
| B | ASP727 |
| B | LYS730 |
| B | PO41001 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 C 1001 |
| Chain | Residue |
| C | LYS250 |
| C | ASP253 |
| C | ASP279 |
| C | ASP283 |
| C | ASP507 |
| C | ASP691 |
| C | LYS730 |
| C | MG1003 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue MG C 1002 |
| Chain | Residue |
| C | ASP507 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 1003 |
| Chain | Residue |
| C | ASP253 |
| C | ASP691 |
| C | ASP723 |
| C | ASP727 |
| C | PO41001 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 D 1001 |
| Chain | Residue |
| D | LYS250 |
| D | ASP253 |
| D | ASP283 |
| D | ASP507 |
| D | ASN534 |
| D | ASP691 |
| D | ASP727 |
| D | LYS730 |
| D | MG1002 |
| D | MG1003 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 1002 |
| Chain | Residue |
| D | ASP279 |
| D | ASP283 |
| D | ASP507 |
| D | PO41001 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 1003 |
| Chain | Residue |
| D | LYS250 |
| D | ASP253 |
| D | ASP727 |
| D | LYS730 |
| D | PO41001 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 296 |
| Details | TOPO_DOM: Intravacuolar => ECO:0000305|PubMed:22456709 |
| Chain | Residue | Details |
| A | GLY2-ASP8 | |
| B | GLY2-ASP8 | |
| B | GLU115-ALA135 | |
| B | GLY217-ASP219 | |
| B | SER313-GLU320 | |
| B | ALA383-SER401 | |
| B | SER473-ALA478 | |
| B | SER564-PRO573 | |
| B | GLY661 | |
| B | GLY759-ILE765 | |
| C | GLY2-ASP8 | |
| A | GLU115-ALA135 | |
| C | GLU115-ALA135 | |
| C | GLY217-ASP219 | |
| C | SER313-GLU320 | |
| C | ALA383-SER401 | |
| C | SER473-ALA478 | |
| C | SER564-PRO573 | |
| C | GLY661 | |
| C | GLY759-ILE765 | |
| D | GLY2-ASP8 | |
| D | GLU115-ALA135 | |
| A | GLY217-ASP219 | |
| D | GLY217-ASP219 | |
| D | SER313-GLU320 | |
| D | ALA383-SER401 | |
| D | SER473-ALA478 | |
| D | SER564-PRO573 | |
| D | GLY661 | |
| D | GLY759-ILE765 | |
| A | SER313-GLU320 | |
| A | ALA383-SER401 | |
| A | SER473-ALA478 | |
| A | SER564-PRO573 | |
| A | GLY661 | |
| A | GLY759-ILE765 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1700 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| A | LEU9-LYS35 | |
| A | VAL448-VAL472 | |
| A | MET479-ILE505 | |
| A | THR535-ALA563 | |
| A | LYS574-LEU602 | |
| A | LYS632-PHE660 | |
| A | VAL662-ALA689 | |
| A | SER733-HIS758 | |
| B | LEU9-LYS35 | |
| B | ALA85-VAL114 | |
| B | LEU136-ILE163 | |
| A | ALA85-VAL114 | |
| B | PHE187-TYR216 | |
| B | TRP220-TYR248 | |
| B | ASP287-ILE312 | |
| B | LEU321-THR346 | |
| B | LYS355-VAL382 | |
| B | TRP402-TYR425 | |
| B | VAL448-VAL472 | |
| B | MET479-ILE505 | |
| B | THR535-ALA563 | |
| B | LYS574-LEU602 | |
| A | LEU136-ILE163 | |
| B | LYS632-PHE660 | |
| B | VAL662-ALA689 | |
| B | SER733-HIS758 | |
| C | LEU9-LYS35 | |
| C | ALA85-VAL114 | |
| C | LEU136-ILE163 | |
| C | PHE187-TYR216 | |
| C | TRP220-TYR248 | |
| C | ASP287-ILE312 | |
| C | LEU321-THR346 | |
| A | PHE187-TYR216 | |
| C | LYS355-VAL382 | |
| C | TRP402-TYR425 | |
| C | VAL448-VAL472 | |
| C | MET479-ILE505 | |
| C | THR535-ALA563 | |
| C | LYS574-LEU602 | |
| C | LYS632-PHE660 | |
| C | VAL662-ALA689 | |
| C | SER733-HIS758 | |
| D | LEU9-LYS35 | |
| A | TRP220-TYR248 | |
| D | ALA85-VAL114 | |
| D | LEU136-ILE163 | |
| D | PHE187-TYR216 | |
| D | TRP220-TYR248 | |
| D | ASP287-ILE312 | |
| D | LEU321-THR346 | |
| D | LYS355-VAL382 | |
| D | TRP402-TYR425 | |
| D | VAL448-VAL472 | |
| D | MET479-ILE505 | |
| A | ASP287-ILE312 | |
| D | THR535-ALA563 | |
| D | LYS574-LEU602 | |
| D | LYS632-PHE660 | |
| D | VAL662-ALA689 | |
| D | SER733-HIS758 | |
| A | LEU321-THR346 | |
| A | LYS355-VAL382 | |
| A | TRP402-TYR425 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 932 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:22456709 |
| Chain | Residue | Details |
| A | VAL36-GLY84 | |
| B | ALA164-ALA186 | |
| B | THR249-GLY286 | |
| B | ASP347-VAL354 | |
| B | THR426-ASN447 | |
| B | SER506-ASN534 | |
| B | LYS603-VAL631 | |
| B | TRP690-THR732 | |
| C | VAL36-GLY84 | |
| C | ALA164-ALA186 | |
| C | THR249-GLY286 | |
| A | ALA164-ALA186 | |
| C | ASP347-VAL354 | |
| C | THR426-ASN447 | |
| C | SER506-ASN534 | |
| C | LYS603-VAL631 | |
| C | TRP690-THR732 | |
| D | VAL36-GLY84 | |
| D | ALA164-ALA186 | |
| D | THR249-GLY286 | |
| D | ASP347-VAL354 | |
| D | THR426-ASN447 | |
| A | THR249-GLY286 | |
| D | SER506-ASN534 | |
| D | LYS603-VAL631 | |
| D | TRP690-THR732 | |
| A | ASP347-VAL354 | |
| A | THR426-ASN447 | |
| A | SER506-ASN534 | |
| A | LYS603-VAL631 | |
| A | TRP690-THR732 | |
| B | VAL36-GLY84 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS250 | |
| A | LYS730 | |
| B | LYS250 | |
| B | LYS730 | |
| C | LYS250 | |
| C | LYS730 | |
| D | LYS250 | |
| D | LYS730 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22456709 |
| Chain | Residue | Details |
| A | ASP253 | |
| B | ASP283 | |
| B | ASP507 | |
| B | ASN534 | |
| B | ASP691 | |
| B | ASP727 | |
| C | ASP253 | |
| C | ASP257 | |
| C | ASP283 | |
| C | ASP507 | |
| C | ASN534 | |
| A | ASP257 | |
| C | ASP691 | |
| C | ASP727 | |
| D | ASP253 | |
| D | ASP257 | |
| D | ASP283 | |
| D | ASP507 | |
| D | ASN534 | |
| D | ASP691 | |
| D | ASP727 | |
| A | ASP283 | |
| A | ASP507 | |
| A | ASN534 | |
| A | ASP691 | |
| A | ASP727 | |
| B | ASP253 | |
| B | ASP257 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 24 |
| Details | SITE: Important for proton transport => ECO:0000305 |
| Chain | Residue | Details |
| A | ARG242 | |
| B | GLU301 | |
| B | ASP731 | |
| B | LYS742 | |
| C | ARG242 | |
| C | ASP287 | |
| C | ASP294 | |
| C | GLU301 | |
| C | ASP731 | |
| C | LYS742 | |
| D | ARG242 | |
| A | ASP287 | |
| D | ASP287 | |
| D | ASP294 | |
| D | GLU301 | |
| D | ASP731 | |
| D | LYS742 | |
| A | ASP294 | |
| A | GLU301 | |
| A | ASP731 | |
| A | LYS742 | |
| B | ARG242 | |
| B | ASP287 | |
| B | ASP294 |
