1VJC
Structure of pig muscle PGK complexed with MgATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004618 | molecular_function | phosphoglycerate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0043531 | molecular_function | ADP binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 418 |
| Chain | Residue |
| A | ATP417 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP A 417 |
| Chain | Residue |
| A | VAL341 |
| A | GLU343 |
| A | ASP374 |
| A | MG418 |
| A | HOH455 |
| A | HOH465 |
| A | HOH470 |
| A | HOH543 |
| A | HOH545 |
| A | GLY213 |
| A | ALA214 |
| A | LYS219 |
| A | GLY237 |
| A | GLY238 |
| A | LEU256 |
| A | GLY312 |
| A | GLY340 |
Functional Information from PROSITE/UniProt
| site_id | PS00111 |
| Number of Residues | 11 |
| Details | PGLYCERATE_KINASE Phosphoglycerate kinase signature. RVVMRvDfNVP |
| Chain | Residue | Details |
| A | ARG17-PRO27 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00558 |
| Chain | Residue | Details |
| A | ASP23 | |
| A | ASP218 | |
| A | GLY238 | |
| A | PRO338 | |
| A | GLY340 | |
| A | GLU343 | |
| A | ASN25 | |
| A | ARG38 | |
| A | HIS62 | |
| A | ARG65 | |
| A | ARG122 | |
| A | ARG170 | |
| A | ALA214 | |
| A | LYS215 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12102622, ECO:0007744|PDB:1KF0 |
| Chain | Residue | Details |
| A | PHE24 | |
| A | LEU63 | |
| A | LYS219 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11178909, ECO:0000269|PubMed:12102622, ECO:0007744|PDB:1HDI, ECO:0007744|PDB:1KF0 |
| Chain | Residue | Details |
| A | VAL26 | |
| A | ILE39 | |
| A | PHE123 | |
| A | ALA171 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11178909, ECO:0007744|PDB:1HDI |
| Chain | Residue | Details |
| A | PRO66 | |
| A | VAL216 | |
| A | THR375 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15035615, ECO:0007744|PDB:1VJC, ECO:0007744|PDB:1VJD |
| Chain | Residue | Details |
| A | ILE220 | |
| A | MET239 | |
| A | LEU313 | |
| A | TRP344 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15035615, ECO:0007744|PDB:1VJD |
| Chain | Residue | Details |
| A | ALA376 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00558 |
| Chain | Residue | Details |
| A | LEU2 | |
| A | ASN4 | |
| A | PRO203 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P09411 |
| Chain | Residue | Details |
| A | LEU6 | |
| A | LYS191 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 7 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00558 |
| Chain | Residue | Details |
| A | LEU11 | |
| A | TYR75 | |
| A | SER86 | |
| A | ILE146 | |
| A | ALA199 | |
| A | ASP267 | |
| A | PHE291 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09411 |
| Chain | Residue | Details |
| A | PHE48 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09411 |
| Chain | Residue | Details |
| A | SER76 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09411 |
| Chain | Residue | Details |
| A | ASP91 | |
| A | ALA361 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00558 |
| Chain | Residue | Details |
| A | ASP97 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-malonyllysine; alternate => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY131 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00558 |
| Chain | Residue | Details |
| A | PHE196 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P00558 |
| Chain | Residue | Details |
| A | VAL216 | |
| A | ILE220 | |
| A | TYR323 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 13pk |
| Chain | Residue | Details |
| A | ARG38 | |
| A | LYS215 | |
| A | GLY373 | |
| A | GLY396 |
