1WPG
Crystal structure of the SR CA2+-ATPase with MGF4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005215 | molecular_function | transporter activity |
| A | 0005388 | molecular_function | P-type calcium transporter activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006816 | biological_process | calcium ion transport |
| A | 0006874 | biological_process | intracellular calcium ion homeostasis |
| A | 0016020 | cellular_component | membrane |
| A | 0016529 | cellular_component | sarcoplasmic reticulum |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0031448 | biological_process | positive regulation of fast-twitch skeletal muscle fiber contraction |
| A | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070588 | biological_process | calcium ion transmembrane transport |
| A | 0106134 | biological_process | positive regulation of cardiac muscle cell contraction |
| A | 1901896 | biological_process | positive regulation of ATPase-coupled calcium transmembrane transporter activity |
| A | 1902082 | biological_process | positive regulation of calcium ion import into sarcoplasmic reticulum |
| A | 1990036 | biological_process | calcium ion import into sarcoplasmic reticulum |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005215 | molecular_function | transporter activity |
| B | 0005388 | molecular_function | P-type calcium transporter activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006816 | biological_process | calcium ion transport |
| B | 0006874 | biological_process | intracellular calcium ion homeostasis |
| B | 0016020 | cellular_component | membrane |
| B | 0016529 | cellular_component | sarcoplasmic reticulum |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0031448 | biological_process | positive regulation of fast-twitch skeletal muscle fiber contraction |
| B | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070588 | biological_process | calcium ion transmembrane transport |
| B | 0106134 | biological_process | positive regulation of cardiac muscle cell contraction |
| B | 1901896 | biological_process | positive regulation of ATPase-coupled calcium transmembrane transporter activity |
| B | 1902082 | biological_process | positive regulation of calcium ion import into sarcoplasmic reticulum |
| B | 1990036 | biological_process | calcium ion import into sarcoplasmic reticulum |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005215 | molecular_function | transporter activity |
| C | 0005388 | molecular_function | P-type calcium transporter activity |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006816 | biological_process | calcium ion transport |
| C | 0006874 | biological_process | intracellular calcium ion homeostasis |
| C | 0016020 | cellular_component | membrane |
| C | 0016529 | cellular_component | sarcoplasmic reticulum |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0031448 | biological_process | positive regulation of fast-twitch skeletal muscle fiber contraction |
| C | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070588 | biological_process | calcium ion transmembrane transport |
| C | 0106134 | biological_process | positive regulation of cardiac muscle cell contraction |
| C | 1901896 | biological_process | positive regulation of ATPase-coupled calcium transmembrane transporter activity |
| C | 1902082 | biological_process | positive regulation of calcium ion import into sarcoplasmic reticulum |
| C | 1990036 | biological_process | calcium ion import into sarcoplasmic reticulum |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005215 | molecular_function | transporter activity |
| D | 0005388 | molecular_function | P-type calcium transporter activity |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006816 | biological_process | calcium ion transport |
| D | 0006874 | biological_process | intracellular calcium ion homeostasis |
| D | 0016020 | cellular_component | membrane |
| D | 0016529 | cellular_component | sarcoplasmic reticulum |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0031448 | biological_process | positive regulation of fast-twitch skeletal muscle fiber contraction |
| D | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070588 | biological_process | calcium ion transmembrane transport |
| D | 0106134 | biological_process | positive regulation of cardiac muscle cell contraction |
| D | 1901896 | biological_process | positive regulation of ATPase-coupled calcium transmembrane transporter activity |
| D | 1902082 | biological_process | positive regulation of calcium ion import into sarcoplasmic reticulum |
| D | 1990036 | biological_process | calcium ion import into sarcoplasmic reticulum |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 997 |
| Chain | Residue |
| A | ASP351 |
| A | THR353 |
| A | ASP703 |
| A | MF4998 |
| A | HOH2100 |
| A | HOH2105 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 997 |
| Chain | Residue |
| B | MF41098 |
| B | HOH3100 |
| B | HOH3105 |
| B | ASP351 |
| B | THR353 |
| B | ASP703 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 997 |
| Chain | Residue |
| C | ASP351 |
| C | THR353 |
| C | ASP703 |
| C | MF41198 |
| C | HOH4100 |
| C | HOH4105 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 997 |
| Chain | Residue |
| D | ASP351 |
| D | THR353 |
| D | ASP703 |
| D | MF41298 |
| D | HOH5100 |
| D | HOH5105 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 1001 |
| Chain | Residue |
| A | LYS205 |
| A | ADP1002 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 1101 |
| Chain | Residue |
| B | ADP1102 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG C 1201 |
| Chain | Residue |
| C | ADP1202 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 1301 |
| Chain | Residue |
| D | LYS205 |
| D | ADP1302 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1000 |
| Chain | Residue |
| A | LEU711 |
| A | LYS712 |
| A | ALA714 |
| A | GLU732 |
| A | HOH2127 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 1100 |
| Chain | Residue |
| B | GLN244 |
| B | LEU711 |
| B | LYS712 |
| B | ALA714 |
| B | GLU732 |
| B | HOH3127 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 1200 |
| Chain | Residue |
| C | GLN244 |
| C | LEU711 |
| C | LYS712 |
| C | ALA714 |
| C | GLU732 |
| C | HOH4127 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 1300 |
| Chain | Residue |
| D | LEU711 |
| D | LYS712 |
| D | ALA714 |
| D | GLU732 |
| D | HOH5127 |
| site_id | BC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MF4 A 998 |
| Chain | Residue |
| A | THR181 |
| A | GLY182 |
| A | GLU183 |
| A | ASP351 |
| A | LYS352 |
| A | THR353 |
| A | THR625 |
| A | GLY626 |
| A | ASP627 |
| A | LYS684 |
| A | ASN706 |
| A | MG997 |
| A | HOH2100 |
| A | HOH2105 |
| site_id | BC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP A 1002 |
| Chain | Residue |
| A | ILE188 |
| A | LYS205 |
| A | PHE487 |
| A | MET494 |
| A | LYS515 |
| A | GLY516 |
| A | ARG560 |
| A | LEU562 |
| A | MG1001 |
| A | HOH2030 |
| A | HOH2046 |
| A | HOH2053 |
| site_id | BC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TG1 A 1003 |
| Chain | Residue |
| A | GLU255 |
| A | GLN259 |
| A | LEU260 |
| A | VAL263 |
| A | ALA306 |
| A | ILE765 |
| A | ASN768 |
| A | LEU828 |
| A | ILE829 |
| A | PHE834 |
| A | TYR837 |
| A | MET838 |
| site_id | BC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MF4 B 1098 |
| Chain | Residue |
| B | LYS684 |
| B | ASN706 |
| B | MG997 |
| B | HOH3100 |
| B | HOH3105 |
| B | THR181 |
| B | GLY182 |
| B | GLU183 |
| B | ASP351 |
| B | LYS352 |
| B | THR353 |
| B | THR625 |
| B | GLY626 |
| B | ASP627 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ADP B 1102 |
| Chain | Residue |
| B | LYS205 |
| B | PHE487 |
| B | MET494 |
| B | LYS515 |
| B | LEU562 |
| B | MG1101 |
| B | HOH3030 |
| B | HOH3046 |
| B | HOH3053 |
| site_id | BC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TG1 B 1103 |
| Chain | Residue |
| B | GLU255 |
| B | PHE256 |
| B | GLN259 |
| B | LEU260 |
| B | VAL263 |
| B | ALA306 |
| B | ASN768 |
| B | VAL769 |
| B | LEU828 |
| B | ILE829 |
| B | PHE834 |
| B | TYR837 |
| B | MET838 |
| site_id | CC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MF4 C 1198 |
| Chain | Residue |
| C | THR181 |
| C | GLY182 |
| C | GLU183 |
| C | ASP351 |
| C | LYS352 |
| C | THR353 |
| C | THR625 |
| C | GLY626 |
| C | ASP627 |
| C | LYS684 |
| C | ASN706 |
| C | MG997 |
| C | HOH4100 |
| C | HOH4105 |
| site_id | CC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP C 1202 |
| Chain | Residue |
| C | LYS205 |
| C | PHE487 |
| C | MET494 |
| C | LYS515 |
| C | GLY516 |
| C | LEU562 |
| C | MG1201 |
| C | HOH4030 |
| C | HOH4046 |
| C | HOH4053 |
| site_id | CC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TG1 C 1203 |
| Chain | Residue |
| C | GLU255 |
| C | PHE256 |
| C | GLN259 |
| C | LEU260 |
| C | VAL263 |
| C | ALA306 |
| C | ASN768 |
| C | VAL769 |
| C | LEU828 |
| C | ILE829 |
| C | PHE834 |
| C | TYR837 |
| C | MET838 |
| site_id | CC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MF4 D 1298 |
| Chain | Residue |
| D | THR181 |
| D | GLY182 |
| D | GLU183 |
| D | ASP351 |
| D | LYS352 |
| D | THR353 |
| D | THR625 |
| D | GLY626 |
| D | ASP627 |
| D | LYS684 |
| D | ASN706 |
| D | MG997 |
| D | HOH5100 |
| D | HOH5105 |
| site_id | CC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP D 1302 |
| Chain | Residue |
| D | ILE188 |
| D | LYS205 |
| D | PHE487 |
| D | MET494 |
| D | LYS515 |
| D | GLY516 |
| D | ARG560 |
| D | LEU562 |
| D | MG1301 |
| D | HOH5030 |
| D | HOH5046 |
| D | HOH5047 |
| D | HOH5053 |
| site_id | CC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TG1 D 1303 |
| Chain | Residue |
| D | GLU255 |
| D | GLN259 |
| D | LEU260 |
| D | VAL263 |
| D | ALA306 |
| D | ILE765 |
| D | ASN768 |
| D | LEU828 |
| D | ILE829 |
| D | PHE834 |
| D | TYR837 |
| D | MET838 |
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 | ASP351-THR357 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2652 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | MET1-SER48 | |
| B | GLU918-ASN930 | |
| C | MET1-SER48 | |
| C | ASN111-LEU253 | |
| C | VAL314-MET757 | |
| C | PHE809-LEU828 | |
| C | GLU918-ASN930 | |
| D | MET1-SER48 | |
| D | ASN111-LEU253 | |
| D | VAL314-MET757 | |
| D | PHE809-LEU828 | |
| A | ASN111-LEU253 | |
| D | GLU918-ASN930 | |
| A | VAL314-MET757 | |
| A | PHE809-LEU828 | |
| A | GLU918-ASN930 | |
| B | MET1-SER48 | |
| B | ASN111-LEU253 | |
| B | VAL314-MET757 | |
| B | PHE809-LEU828 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | LEU49-ALA69 | |
| B | LEU49-ALA69 | |
| C | LEU49-ALA69 | |
| D | LEU49-ALA69 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 432 |
| Details | TOPO_DOM: Lumenal => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | CYS70-VAL89 | |
| B | VAL950-LEU964 | |
| C | CYS70-VAL89 | |
| C | ILE274-TYR295 | |
| C | THR778-LEU787 | |
| C | ALA852-MET897 | |
| C | VAL950-LEU964 | |
| D | CYS70-VAL89 | |
| D | ILE274-TYR295 | |
| D | THR778-LEU787 | |
| D | ALA852-MET897 | |
| A | ILE274-TYR295 | |
| D | VAL950-LEU964 | |
| A | THR778-LEU787 | |
| A | ALA852-MET897 | |
| A | VAL950-LEU964 | |
| B | CYS70-VAL89 | |
| B | ILE274-TYR295 | |
| B | THR778-LEU787 | |
| B | ALA852-MET897 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | GLU90-ARG110 | |
| B | GLU90-ARG110 | |
| C | GLU90-ARG110 | |
| D | GLU90-ARG110 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 76 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | ASP254-LEU273 | |
| B | ASP254-LEU273 | |
| C | ASP254-LEU273 | |
| D | ASP254-LEU273 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 68 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | PHE296-ALA313 | |
| B | PHE296-ALA313 | |
| C | PHE296-ALA313 | |
| D | PHE296-ALA313 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 76 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | LYS758-LEU777 | |
| B | LYS758-LEU777 | |
| C | LYS758-LEU777 | |
| D | LYS758-LEU777 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | ILE788-GLY808 | |
| B | ILE788-GLY808 | |
| C | ILE788-GLY808 | |
| D | ILE788-GLY808 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 88 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | ILE829-ALA851 | |
| B | ILE829-ALA851 | |
| C | ILE829-ALA851 | |
| D | ILE829-ALA851 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 76 |
| Details | TRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | THR898-SER917 | |
| B | THR898-SER917 | |
| C | THR898-SER917 | |
| D | THR898-SER917 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 72 |
| Details | TRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | ILE931-TYR949 | |
| B | ILE931-TYR949 | |
| C | ILE931-TYR949 | |
| D | ILE931-TYR949 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:10864315 |
| Chain | Residue | Details |
| A | THR965-LYS985 | |
| B | THR965-LYS985 | |
| C | THR965-LYS985 | |
| D | THR965-LYS985 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | ACT_SITE: 4-aspartylphosphate intermediate => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:18075584 |
| Chain | Residue | Details |
| A | ASP351 | |
| B | ASP351 | |
| C | ASP351 | |
| D | ASP351 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8 |
| Chain | Residue | Details |
| A | VAL304 | |
| B | VAL304 | |
| C | VAL304 | |
| D | VAL304 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8 |
| Chain | Residue | Details |
| A | ALA305 | |
| B | ALA305 | |
| C | ALA305 | |
| D | ALA305 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU |
| Chain | Residue | Details |
| A | ILE307 | |
| B | ILE307 | |
| C | ILE307 | |
| D | ILE307 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8 |
| Chain | Residue | Details |
| A | GLU309 | |
| B | GLU309 | |
| C | GLU309 | |
| D | GLU309 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:1WPG, ECO:0007744|PDB:1XP5, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:2ZBE, ECO:0007744|PDB:2ZBF, ECO:0007744|PDB:2ZBG, ECO:0007744|PDB:3AR8, ECO:0007744|PDB:3AR9, ECO:0007744|PDB:3B9B, ECO:0007744|PDB:3B9R, ECO:0007744|PDB:3FGO, ECO:0007744|PDB:3FPB, ECO:0007744|PDB:3N5K, ECO:0007744|PDB:4BEW, ECO:0007744|PDB:5A3Q, ECO:0007744|PDB:5A3S |
| Chain | Residue | Details |
| A | ASP351 | |
| D | ASP351 | |
| D | THR353 | |
| D | ASP703 | |
| A | THR353 | |
| A | ASP703 | |
| B | ASP351 | |
| B | THR353 | |
| B | ASP703 | |
| C | ASP351 | |
| C | THR353 | |
| C | ASP703 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:2BY4, ECO:0007744|PDB:2C88, ECO:0007744|PDB:2DQS, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3AR3, ECO:0007744|PDB:4UU1, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA8 |
| Chain | Residue | Details |
| A | GLU442 | |
| B | GLU442 | |
| C | GLU442 | |
| D | GLU442 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:1WPG, ECO:0007744|PDB:2DQS, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3B9R, ECO:0007744|PDB:3FGO, ECO:0007744|PDB:3FPB, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4BEW, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA8 |
| Chain | Residue | Details |
| A | ARG489 | |
| B | ARG489 | |
| C | ARG489 | |
| D | ARG489 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:2BY4, ECO:0007744|PDB:2C8K, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4UU1, ECO:0007744|PDB:4XOU |
| Chain | Residue | Details |
| A | LYS515 | |
| B | LYS515 | |
| C | LYS515 | |
| D | LYS515 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2BY4, ECO:0007744|PDB:2C88, ECO:0007744|PDB:2C8K, ECO:0007744|PDB:2DQS, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3B9R, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4H1W, ECO:0007744|PDB:4UU1, ECO:0007744|PDB:4XOU |
| Chain | Residue | Details |
| A | ARG560 | |
| B | ARG560 | |
| C | ARG560 | |
| D | ARG560 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA8 |
| Chain | Residue | Details |
| A | THR625 | |
| B | THR625 | |
| C | THR625 | |
| D | THR625 |
| site_id | SWS_FT_FI24 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4UU1, ECO:0007744|PDB:4XOU |
| Chain | Residue | Details |
| A | GLY626 | |
| B | GLY626 | |
| C | GLY626 | |
| D | GLY626 |
| site_id | SWS_FT_FI25 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0007744|PDB:1T5T |
| Chain | Residue | Details |
| A | ASP627 | |
| B | ASP627 | |
| C | ASP627 | |
| D | ASP627 |
| site_id | SWS_FT_FI26 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3FGO, ECO:0007744|PDB:3FPB, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4BEW, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA8 |
| Chain | Residue | Details |
| A | ARG678 | |
| B | ARG678 | |
| C | ARG678 | |
| D | ARG678 |
| site_id | SWS_FT_FI27 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU |
| Chain | Residue | Details |
| A | LYS684 | |
| B | LYS684 | |
| C | LYS684 | |
| D | LYS684 |
| site_id | SWS_FT_FI28 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU |
| Chain | Residue | Details |
| A | ASN706 | |
| B | ASN706 | |
| C | ASN706 | |
| D | ASN706 |
| site_id | SWS_FT_FI29 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8 |
| Chain | Residue | Details |
| A | ASN768 | |
| A | THR799 | |
| B | ASN768 | |
| B | THR799 | |
| C | ASN768 | |
| C | THR799 | |
| D | ASN768 | |
| D | THR799 |
| site_id | SWS_FT_FI30 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8 |
| Chain | Residue | Details |
| A | GLU771 | |
| B | GLU771 | |
| C | GLU771 | |
| D | GLU771 |
| site_id | SWS_FT_FI31 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8 |
| Chain | Residue | Details |
| A | ASN796 | |
| B | ASN796 | |
| C | ASN796 | |
| D | ASN796 |
| site_id | SWS_FT_FI32 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8 |
| Chain | Residue | Details |
| A | ASP800 | |
| B | ASP800 | |
| C | ASP800 | |
| D | ASP800 |
| site_id | SWS_FT_FI33 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU |
| Chain | Residue | Details |
| A | GLU908 | |
| B | GLU908 | |
| C | GLU908 | |
| D | GLU908 |
| site_id | SWS_FT_FI34 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q64578 |
| Chain | Residue | Details |
| A | THR441 | |
| A | THR569 | |
| B | THR441 | |
| B | THR569 | |
| C | THR441 | |
| C | THR569 | |
| D | THR441 | |
| D | THR569 |
| site_id | SWS_FT_FI35 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q64578 |
| Chain | Residue | Details |
| A | SER581 | |
| B | SER581 | |
| C | SER581 | |
| D | SER581 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 849 |
| Chain | Residue | Details |
| A | ASP351 | covalent catalysis |
| A | ASP703 | metal ligand |
| A | ASP707 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 849 |
| Chain | Residue | Details |
| B | ASP351 | covalent catalysis |
| B | ASP703 | metal ligand |
| B | ASP707 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 849 |
| Chain | Residue | Details |
| C | ASP351 | covalent catalysis |
| C | ASP703 | metal ligand |
| C | ASP707 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 849 |
| Chain | Residue | Details |
| D | ASP351 | covalent catalysis |
| D | ASP703 | metal ligand |
| D | ASP707 | metal ligand |
