8IT4
Phosphoglycerate mutase 1 complexed with a covalent inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004082 | molecular_function | bisphosphoglycerate mutase activity |
| A | 0004619 | molecular_function | phosphoglycerate mutase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
| A | 0061621 | biological_process | canonical glycolysis |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| B | 0004082 | molecular_function | bisphosphoglycerate mutase activity |
| B | 0004619 | molecular_function | phosphoglycerate mutase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| B | 0019901 | molecular_function | protein kinase binding |
| B | 0034774 | cellular_component | secretory granule lumen |
| B | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
| B | 0061621 | biological_process | canonical glycolysis |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PROSITE/UniProt
| site_id | PS00175 |
| Number of Residues | 10 |
| Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsAwN |
| Chain | Residue | Details |
| A | LEU8-ASN17 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:23653202, ECO:0000305|PubMed:15883004 |
| Chain | Residue | Details |
| A | HIS11 | |
| B | HIS103 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15883004 |
| Chain | Residue | Details |
| A | GLU89 | |
| B | GLU181 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15883004, ECO:0000269|PubMed:23653202 |
| Chain | Residue | Details |
| A | ARG10 | |
| A | SER23 | |
| A | LYS100 | |
| B | ARG102 | |
| B | SER115 | |
| B | LYS192 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q3JWH7 |
| Chain | Residue | Details |
| A | ARG62 | |
| A | GLY187 | |
| B | ARG154 | |
| B | GLY279 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15883004 |
| Chain | Residue | Details |
| A | GLU89 | |
| A | ARG116 | |
| B | GLU181 | |
| B | ARG208 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950 |
| Chain | Residue | Details |
| A | HIS186 | |
| B | HIS278 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER14 | |
| B | SER106 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER23 | |
| B | SER115 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:23653202 |
| Chain | Residue | Details |
| A | TYR26 | |
| B | TYR118 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER31 | |
| B | SER123 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBJ1 |
| Chain | Residue | Details |
| A | LYS106 | |
| B | LYS198 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9DBJ1 |
| Chain | Residue | Details |
| A | SER118 | |
| B | SER210 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBJ1 |
| Chain | Residue | Details |
| A | LYS251 | |
| B | LYS343 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22157007 |
| Chain | Residue | Details |
| A | LYS253 | |
| A | LYS254 | |
| B | LYS345 | |
| B | LYS346 |
