4PGM
SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004619 | molecular_function | phosphoglycerate mutase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005741 | cellular_component | mitochondrial outer membrane |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0005829 | cellular_component | cytosol |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| A | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004619 | molecular_function | phosphoglycerate mutase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005741 | cellular_component | mitochondrial outer membrane |
| B | 0005758 | cellular_component | mitochondrial intermembrane space |
| B | 0005829 | cellular_component | cytosol |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| B | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004619 | molecular_function | phosphoglycerate mutase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005741 | cellular_component | mitochondrial outer membrane |
| C | 0005758 | cellular_component | mitochondrial intermembrane space |
| C | 0005829 | cellular_component | cytosol |
| C | 0006094 | biological_process | gluconeogenesis |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| C | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004619 | molecular_function | phosphoglycerate mutase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005741 | cellular_component | mitochondrial outer membrane |
| D | 0005758 | cellular_component | mitochondrial intermembrane space |
| D | 0005829 | cellular_component | cytosol |
| D | 0006094 | biological_process | gluconeogenesis |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| D | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
Functional Information from PDB Data
| site_id | CIC |
| Number of Residues | 4 |
| Details | CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME. |
| Chain | Residue |
| A | HIS8 |
| A | HIS181 |
| A | ARG7 |
| A | ARG59 |
Functional Information from PROSITE/UniProt
| site_id | PS00175 |
| Number of Residues | 10 |
| Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LvRHGQsEwN |
| Chain | Residue | Details |
| A | LEU5-ASN14 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:10064712, ECO:0000269|PubMed:10531478, ECO:0000269|PubMed:6115412, ECO:0000269|PubMed:9512715 |
| Chain | Residue | Details |
| A | GLY9 | |
| B | GLY9 | |
| C | GLY9 | |
| D | GLY9 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10064712 |
| Chain | Residue | Details |
| A | ARG87 | |
| B | ARG87 | |
| C | ARG87 | |
| D | ARG87 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:10531478, ECO:0000269|PubMed:6115412 |
| Chain | Residue | Details |
| A | HIS8 | |
| B | HIS8 | |
| C | HIS8 | |
| D | HIS8 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:10531478 |
| Chain | Residue | Details |
| A | GLY21 | |
| B | GLY21 | |
| C | GLY21 | |
| D | GLY21 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10531478 |
| Chain | Residue | Details |
| A | ALA60 | |
| B | ALA60 | |
| C | ALA60 | |
| D | ALA60 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:6115412 |
| Chain | Residue | Details |
| A | ARG87 | |
| A | ASN183 | |
| B | ARG87 | |
| B | ASN183 | |
| C | ARG87 | |
| C | ASN183 | |
| D | ARG87 | |
| D | ASN183 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10369755 |
| Chain | Residue | Details |
| A | ALA98 | |
| A | ARG114 | |
| B | ALA98 | |
| B | ARG114 | |
| C | ALA98 | |
| C | ARG114 | |
| D | ALA98 | |
| D | ARG114 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:10064712 |
| Chain | Residue | Details |
| A | GLY182 | |
| B | GLY182 | |
| C | GLY182 | |
| D | GLY182 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358 |
| Chain | Residue | Details |
| A | GLU12 | |
| A | LEU185 | |
| B | GLU12 | |
| B | LEU185 | |
| C | GLU12 | |
| C | LEU185 | |
| D | GLU12 | |
| D | LEU185 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | PRO49 | |
| B | PRO49 | |
| C | PRO49 | |
| D | PRO49 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | PHE116 | |
| B | PHE116 | |
| C | PHE116 | |
| D | PHE116 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | SER127 | |
| B | SER127 | |
| C | SER127 | |
| D | SER127 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | PRO128 | |
| B | PRO128 | |
| C | PRO128 | |
| D | PRO128 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | ASP197 | |
| B | ASP197 | |
| C | ASP197 | |
| D | ASP197 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 28 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
| Chain | Residue | Details |
| A | GLY31 | |
| B | LEU57 | |
| B | ALA71 | |
| B | TYR139 | |
| B | THR175 | |
| B | HIS191 | |
| C | GLY31 | |
| C | LEU57 | |
| C | ALA71 | |
| C | TYR139 | |
| C | THR175 | |
| C | HIS191 | |
| D | GLY31 | |
| D | LEU57 | |
| D | ALA71 | |
| D | TYR139 | |
| D | THR175 | |
| D | HIS191 | |
| A | LEU57 | |
| A | ALA71 | |
| A | TYR139 | |
| A | THR175 | |
| A | HIS191 | |
| B | GLY31 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| A | HIS181 | |
| A | HIS8 | |
| A | GLU86 | |
| A | ARG59 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| B | HIS181 | |
| B | HIS8 | |
| B | GLU86 | |
| B | ARG59 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| C | HIS181 | |
| C | HIS8 | |
| C | GLU86 | |
| C | ARG59 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| D | HIS181 | |
| D | HIS8 | |
| D | GLU86 | |
| D | ARG59 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 504 |
| Chain | Residue | Details |
| A | GLY9 | covalent catalysis |
| A | ALA60 | electrostatic stabiliser |
| A | ARG87 | proton donor, proton shuttle (general acid/base) |
| A | GLY182 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 504 |
| Chain | Residue | Details |
| B | GLY9 | covalent catalysis |
| B | ALA60 | electrostatic stabiliser |
| B | ARG87 | proton donor, proton shuttle (general acid/base) |
| B | GLY182 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 504 |
| Chain | Residue | Details |
| C | GLY9 | covalent catalysis |
| C | ALA60 | electrostatic stabiliser |
| C | ARG87 | proton donor, proton shuttle (general acid/base) |
| C | GLY182 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 504 |
| Chain | Residue | Details |
| D | GLY9 | covalent catalysis |
| D | ALA60 | electrostatic stabiliser |
| D | ARG87 | proton donor, proton shuttle (general acid/base) |
| D | GLY182 | electrostatic stabiliser |
