5VEC
Crystal Structure of the R515L 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 | 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 | 3 |
Details | binding site for residue SO4 A 601 |
Chain | Residue |
A | ARG503 |
A | SER505 |
A | GLY506 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 602 |
Chain | Residue |
A | ASN179 |
A | LYS470 |
A | ARG491 |
A | HOH862 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 603 |
Chain | Residue |
A | PRO244 |
A | ASN246 |
A | HOH724 |
A | ARG217 |
A | ARG221 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 604 |
Chain | Residue |
A | ARG23 |
A | HOH704 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG A 605 |
Chain | Residue |
A | SER117 |
A | ASP288 |
A | ASP290 |
A | ASP292 |
A | HOH726 |
A | HOH766 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue GOL A 606 |
Chain | Residue |
A | PRO244 |
A | ALA245 |
A | HOH714 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue GOL A 607 |
Chain | Residue |
A | PHE65 |
A | TYR66 |
A | MET67 |
A | LYS68 |
A | GLU69 |
A | GLU255 |
A | HOH723 |
A | HOH819 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL A 608 |
Chain | Residue |
A | GLU432 |
A | VAL433 |
A | GLU434 |
A | THR553 |
A | ARG555 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 601 |
Chain | Residue |
B | ARG503 |
B | SER505 |
B | GLY506 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 602 |
Chain | Residue |
B | ARG293 |
B | ARG427 |
B | HOH809 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MG B 603 |
Chain | Residue |
B | SER117 |
B | ASP288 |
B | ASP290 |
B | ASP292 |
B | HOH720 |
B | HOH742 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue GOL B 604 |
Chain | Residue |
B | THR19 |
B | SER20 |
B | GLY358 |
B | TRP359 |
B | GLU376 |
B | GOL605 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue GOL B 605 |
Chain | Residue |
B | THR19 |
B | LYS130 |
B | PRO138 |
B | ASP292 |
B | TRP359 |
B | LYS389 |
B | GOL604 |
B | HOH870 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue GOL B 606 |
Chain | Residue |
B | GLN41 |
B | SER45 |
B | ARG52 |
B | ASN81 |
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 |