1C47
BINDING DRIVEN STRUCTURAL CHANGES IN CRYSTALINE PHOSPHOGLUCOMUTASE ASSOCIATED WITH CHEMICAL REACTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004614 | molecular_function | phosphoglucomutase activity |
| 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 | 0016529 | cellular_component | sarcoplasmic reticulum |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071704 | biological_process | organic substance metabolic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004614 | molecular_function | phosphoglucomutase activity |
| 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 | 0016529 | cellular_component | sarcoplasmic reticulum |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071704 | biological_process | organic substance metabolic process |
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 | GLY110-PRO119 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Phosphoserine intermediate => ECO:0000269|PubMed:5669853 |
| Chain | Residue | Details |
| A | SER116 | |
| B | SER116 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1C47 |
| Chain | Residue | Details |
| A | THR356 | |
| A | GLU375 | |
| A | SER377 | |
| A | LYS388 | |
| B | ARG22 | |
| B | ARG292 | |
| B | THR356 | |
| B | GLU375 | |
| B | SER377 | |
| B | LYS388 | |
| A | ARG22 | |
| A | ARG292 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: via phosphate group => ECO:0000269|PubMed:15299905, ECO:0007744|PDB:3PMG |
| Chain | Residue | Details |
| A | SER116 | |
| B | SER116 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15299905, ECO:0007744|PDB:3PMG |
| Chain | Residue | Details |
| A | ASP291 | |
| A | ASP287 | |
| A | ASP289 | |
| B | ASP287 | |
| B | ASP289 | |
| B | ASP291 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P36871 |
| Chain | Residue | Details |
| A | LYS15 | |
| B | LYS15 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9D0F9 |
| Chain | Residue | Details |
| B | THR114 | |
| B | THR506 | |
| A | THR114 | |
| A | THR506 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15299905, ECO:0007744|PDB:3PMG |
| Chain | Residue | Details |
| A | SER116 | |
| B | SER116 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 10 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P38652 |
| Chain | Residue | Details |
| A | SER540 | |
| B | SER133 | |
| B | SER212 | |
| B | SER368 | |
| B | SER484 | |
| B | SER540 | |
| A | SER133 | |
| A | SER212 | |
| A | SER368 | |
| A | SER484 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P36871 |
| Chain | Residue | Details |
| A | THR184 | |
| B | THR184 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D0F9 |
| Chain | Residue | Details |
| A | LYS348 | |
| B | LYS348 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9D0F9 |
| Chain | Residue | Details |
| A | TYR352 | |
| B | TYR352 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P36871 |
| Chain | Residue | Details |
| A | SER508 | |
| B | SER377 | |
| B | SER504 | |
| B | SER508 | |
| A | SER377 | |
| A | SER504 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9D0F9 |
| Chain | Residue | Details |
| A | LYS418 | |
| B | LYS418 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by PAK1 => ECO:0000250|UniProtKB:P36871 |
| Chain | Residue | Details |
| A | THR466 | |
| B | THR466 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 352 |
| Chain | Residue | Details |
| A | SER116 | activator, covalently attached, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | HIS117 | proton acceptor, proton donor |
| A | ASP287 | metal ligand |
| A | ASP289 | metal ligand |
| A | ASP291 | metal ligand |
| A | ARG292 | electrostatic stabiliser |
| A | LYS388 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 352 |
| Chain | Residue | Details |
| B | SER116 | activator, covalently attached, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | HIS117 | proton acceptor, proton donor |
| B | ASP287 | metal ligand |
| B | ASP289 | metal ligand |
| B | ASP291 | metal ligand |
| B | ARG292 | electrostatic stabiliser |
| B | LYS388 | proton acceptor, proton donor |
