5Y64
Phosphoglycerate mutase 1 H11 phosphorylated form complexed with KH1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0003824 | molecular_function | catalytic activity |
| 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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004082 | molecular_function | bisphosphoglycerate mutase activity |
| C | 0004619 | molecular_function | phosphoglycerate mutase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006094 | biological_process | gluconeogenesis |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| C | 0019901 | molecular_function | protein kinase binding |
| C | 0034774 | cellular_component | secretory granule lumen |
| C | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
| C | 0061621 | biological_process | canonical glycolysis |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 301 |
| Chain | Residue |
| B | TRP68 |
| B | ARG83 |
| C | TRP68 |
| C | ARG83 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue MES C 301 |
| Chain | Residue |
| C | GLY24 |
| C | ARG62 |
| C | GLU89 |
| C | TYR92 |
| C | 8LF302 |
| C | HOH410 |
| C | NEP11 |
| C | ASN17 |
| C | ARG21 |
| C | PHE22 |
| C | SER23 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue 8LF C 302 |
| Chain | Residue |
| C | ASN20 |
| C | ARG21 |
| C | PHE22 |
| C | ARG90 |
| C | LYS100 |
| C | TRP115 |
| C | ARG116 |
| C | MES301 |
| C | HOH402 |
Functional Information from PROSITE/UniProt
| site_id | PS00175 |
| Number of Residues | 10 |
| Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsAwN |
| Chain | Residue | Details |
| B | LEU8-ASN17 | |
| C | LEU8-ASN17 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:23653202, ECO:0000305|PubMed:15883004 |
| Chain | Residue | Details |
| C | NEP11 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15883004 |
| Chain | Residue | Details |
| C | GLU89 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15883004, ECO:0000269|PubMed:23653202 |
| Chain | Residue | Details |
| C | ARG10 | |
| C | SER23 | |
| C | LYS100 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q3JWH7 |
| Chain | Residue | Details |
| C | ARG62 | |
| C | GLY187 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15883004 |
| Chain | Residue | Details |
| C | GLU89 | |
| C | ARG116 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950 |
| Chain | Residue | Details |
| C | HIS186 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| 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 |
| C | SER14 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| C | SER23 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:23653202 |
| Chain | Residue | Details |
| C | TYR26 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| C | SER31 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBJ1 |
| Chain | Residue | Details |
| C | LYS106 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9DBJ1 |
| Chain | Residue | Details |
| C | SER118 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBJ1 |
| Chain | Residue | Details |
| C | LYS251 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22157007 |
| Chain | Residue | Details |
| C | LYS253 | |
| C | LYS254 |
