5VIN
Crystal Structure of the R515Q missense variant of human PGM1
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 | 0005980 | biological_process | glycogen catabolic 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, Leloir pathway |
| 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 | 0005980 | biological_process | glycogen catabolic 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, Leloir pathway |
| 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 | 4 |
| Details | binding site for residue SO4 A 601 |
| Chain | Residue |
| A | THR19 |
| A | GLY358 |
| A | TRP359 |
| A | HOH712 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 602 |
| Chain | Residue |
| A | HIS118 |
| A | ARG293 |
| A | ARG427 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 603 |
| Chain | Residue |
| A | LYS68 |
| A | GLU69 |
| A | GLU255 |
| A | TYR66 |
| A | MET67 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | GLY259 |
| A | HIS260 |
| A | HIS261 |
| A | TYR268 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | SER31 |
| A | SER32 |
| A | ALA33 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 606 |
| Chain | Residue |
| A | ARG555 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 607 |
| Chain | Residue |
| A | PRO123 |
| A | ASN124 |
| A | GLY125 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 608 |
| Chain | Residue |
| A | PRO244 |
| A | ALA245 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 609 |
| Chain | Residue |
| A | LYS470 |
| A | ARG491 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 610 |
| Chain | Residue |
| A | ARG217 |
| A | ARG221 |
| A | PRO244 |
| A | ASN246 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 611 |
| Chain | Residue |
| A | ARG85 |
| A | HOH728 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue GOL A 612 |
| Chain | Residue |
| A | HIS260 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue CO A 614 |
| Chain | Residue |
| A | SER117 |
| A | ASP288 |
| A | ASP290 |
| A | ASP292 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 601 |
| Chain | Residue |
| B | ARG427 |
| B | GOL606 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 602 |
| Chain | Residue |
| B | THR19 |
| B | SER20 |
| B | GLY358 |
| B | TRP359 |
| B | LYS389 |
| B | HOH702 |
| B | HOH716 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 603 |
| Chain | Residue |
| A | SER-1 |
| A | ASN0 |
| B | SER206 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 604 |
| Chain | Residue |
| B | PRO244 |
| B | ALA245 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 605 |
| Chain | Residue |
| B | GLY18 |
| B | THR19 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 606 |
| Chain | Residue |
| B | ARG503 |
| B | SER505 |
| B | THR507 |
| B | SO4601 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue CO B 607 |
| Chain | Residue |
| B | SER117 |
| B | ASP288 |
| B | ASP290 |
| B | ASP292 |
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 | Active site: {"description":"Phosphoserine intermediate","evidences":[{"source":"PubMed","id":"25288802","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00949","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via phosphate groupe","evidences":[{"source":"PubMed","id":"25288802","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26972339","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EPC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F9C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"25288802","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P38652","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by PAK1","evidences":[{"source":"PubMed","id":"15378030","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
