5EPC
Crystal structure of wild-type human phosphoglucomutase 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004614 | molecular_function | phosphoglucomutase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006006 | biological_process | glucose metabolic process |
| 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 | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1904724 | cellular_component | tertiary granule lumen |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004614 | molecular_function | phosphoglucomutase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006006 | biological_process | glucose metabolic process |
| 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 | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 1904724 | cellular_component | tertiary granule lumen |
| B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | SER117 |
| A | ASP288 |
| A | ASP290 |
| A | ASP292 |
| A | HOH771 |
| A | HOH878 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 602 |
| Chain | Residue |
| A | ARG515 |
| A | GOL611 |
| A | ARG503 |
| A | SER505 |
| A | GLY506 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 603 |
| Chain | Residue |
| A | ASN179 |
| A | LYS470 |
| A | ARG491 |
| A | HOH819 |
| A | HOH925 |
| A | HOH1020 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | SER20 |
| A | ARG23 |
| A | SER117 |
| A | HIS118 |
| A | ARG293 |
| A | HOH724 |
| A | HOH878 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | ARG85 |
| A | ILE106 |
| A | HOH706 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 606 |
| Chain | Residue |
| A | ARG217 |
| A | ARG221 |
| A | PRO244 |
| A | ASN246 |
| A | HOH711 |
| A | HOH734 |
| A | HOH980 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 607 |
| Chain | Residue |
| A | TYR66 |
| A | MET67 |
| A | LYS68 |
| A | GLU69 |
| A | GLU255 |
| A | HOH702 |
| A | HOH714 |
| A | HOH972 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 608 |
| Chain | Residue |
| A | PHE303 |
| A | ASN305 |
| A | ARG422 |
| A | PHE424 |
| A | PHE425 |
| A | HOH762 |
| A | HOH851 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 609 |
| Chain | Residue |
| A | ASN135 |
| A | PRO140 |
| A | LYS360 |
| A | GLY363 |
| A | ASN364 |
| A | ASP367 |
| A | HOH767 |
| A | HOH786 |
| A | HOH836 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 610 |
| Chain | Residue |
| A | TYR428 |
| A | GLN533 |
| A | THR556 |
| A | PRO558 |
| A | HOH782 |
| A | HOH810 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 611 |
| Chain | Residue |
| A | GLU377 |
| A | ARG427 |
| A | ARG515 |
| A | TYR517 |
| A | SO4602 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 601 |
| Chain | Residue |
| B | SER117 |
| B | ASP288 |
| B | ASP290 |
| B | ASP292 |
| B | HOH851 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 602 |
| Chain | Residue |
| B | ARG503 |
| B | SER505 |
| B | ARG515 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 603 |
| Chain | Residue |
| B | ARG85 |
| B | ILE106 |
| B | HOH862 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 604 |
| Chain | Residue |
| B | SER20 |
| B | SER117 |
| B | HIS118 |
| B | ARG293 |
| B | HOH706 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 605 |
| Chain | Residue |
| B | ARG64 |
| B | PHE65 |
| B | TYR66 |
| B | MET67 |
| B | LYS68 |
| B | GLU69 |
| B | GLU255 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 606 |
| Chain | Residue |
| B | GLN90 |
| B | ASN91 |
| B | ASP190 |
| B | SER191 |
| B | PRO231 |
| B | LYS235 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 607 |
| Chain | Residue |
| B | ASN305 |
| B | ARG422 |
| B | PHE424 |
| B | PHE425 |
| B | HOH787 |
| B | PHE303 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 608 |
| Chain | Residue |
| A | ASP14 |
| A | VAL28 |
| A | TYR35 |
Functional Information from PROSITE/UniProt
| site_id | PS00710 |
| Number of Residues | 10 |
| Details | PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GIiLTASHNP |
| Chain | Residue | Details |
| A | GLY111-PRO120 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Phosphoserine intermediate => ECO:0000269|PubMed:25288802 |
| Chain | Residue | Details |
| A | SER117 | |
| B | SER117 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00949 |
| Chain | Residue | Details |
| A | ARG23 | |
| B | GLU376 | |
| B | SER378 | |
| B | LYS389 | |
| A | ARG293 | |
| A | THR357 | |
| A | GLU376 | |
| A | SER378 | |
| A | LYS389 | |
| B | ARG23 | |
| B | ARG293 | |
| B | THR357 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: via phosphate groupe => ECO:0000269|PubMed:25288802 |
| Chain | Residue | Details |
| A | SER117 | |
| B | SER117 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26972339, ECO:0007744|PDB:5EPC, ECO:0007744|PDB:5F9C |
| Chain | Residue | Details |
| A | ASP288 | |
| A | ASP290 | |
| A | ASP292 | |
| B | ASP288 | |
| B | ASP290 | |
| B | ASP292 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS16 | |
| B | LYS16 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9D0F9 |
| Chain | Residue | Details |
| A | THR115 | |
| A | THR507 | |
| B | THR115 | |
| B | THR507 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:25288802, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | SER117 | |
| B | SER117 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P38652 |
| Chain | Residue | Details |
| A | SER134 | |
| B | SER477 | |
| B | SER485 | |
| B | SER541 | |
| A | SER213 | |
| A | SER369 | |
| A | SER477 | |
| A | SER485 | |
| A | SER541 | |
| B | SER134 | |
| B | SER213 | |
| B | SER369 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR185 | |
| B | THR185 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 10 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER201 | |
| B | SER509 | |
| A | SER206 | |
| A | SER378 | |
| A | SER505 | |
| A | SER509 | |
| B | SER201 | |
| B | SER206 | |
| B | SER378 | |
| B | SER505 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D0F9 |
| Chain | Residue | Details |
| A | LYS349 | |
| B | LYS349 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9D0F9 |
| Chain | Residue | Details |
| A | TYR353 | |
| B | TYR353 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9D0F9 |
| Chain | Residue | Details |
| A | LYS419 | |
| B | LYS419 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by PAK1 => ECO:0000269|PubMed:15378030 |
| Chain | Residue | Details |
| A | THR467 | |
| B | THR467 |
