1C4G
PHOSPHOGLUCOMUTASE VANADATE BASED TRANSITION STATE ANALOG COMPLEX
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 |
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 |
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 | ARG22 | |
B | GLU375 | |
B | SER377 | |
B | LYS388 | |
A | ARG292 | |
A | THR356 | |
A | GLU375 | |
A | SER377 | |
A | LYS388 | |
B | ARG22 | |
B | ARG292 | |
B | THR356 |
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 | ASP287 | |
A | ASP289 | |
A | ASP291 | |
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 |
A | THR114 | |
A | THR506 | |
B | THR114 | |
B | 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 | SER133 | |
B | SER540 | |
A | SER212 | |
A | SER368 | |
A | SER484 | |
A | SER540 | |
B | SER133 | |
B | SER212 | |
B | SER368 | |
B | 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 | SER377 | |
A | SER504 | |
A | SER508 | |
B | SER377 | |
B | SER504 | |
B | SER508 |
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 |