6SNQ
Crystal structures of human PGM1 isoform 2
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 |
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 | GLY129-PRO138 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Phosphoserine intermediate => ECO:0000269|PubMed:25288802 |
Chain | Residue | Details |
A | SEP135 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00949 |
Chain | Residue | Details |
A | ARG41 | |
A | ARG311 | |
A | THR375 | |
A | GLU394 | |
A | SER396 | |
A | LYS407 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: via phosphate groupe => ECO:0000269|PubMed:25288802 |
Chain | Residue | Details |
A | SEP135 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26972339, ECO:0007744|PDB:5EPC, ECO:0007744|PDB:5F9C |
Chain | Residue | Details |
A | ASP306 | |
A | ASP308 | |
A | ASP310 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS34 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9D0F9 |
Chain | Residue | Details |
A | THR133 | |
A | THR525 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:25288802, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
A | SEP135 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P38652 |
Chain | Residue | Details |
A | SER152 | |
A | SER231 | |
A | SER387 | |
A | SER495 | |
A | SER503 | |
A | SER559 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | THR203 |
site_id | SWS_FT_FI10 |
Number of Residues | 5 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER219 | |
A | SER224 | |
A | SER396 | |
A | SER523 | |
A | SER527 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D0F9 |
Chain | Residue | Details |
A | LYS367 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9D0F9 |
Chain | Residue | Details |
A | TYR371 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9D0F9 |
Chain | Residue | Details |
A | LYS437 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by PAK1 => ECO:0000269|PubMed:15378030 |
Chain | Residue | Details |
A | THR485 |