3C3A
Crystal Structure of human phosphoglycerate kinase bound to 3-phosphoglycerate and L-ADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004618 | molecular_function | phosphoglycerate kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005615 | cellular_component | extracellular space |
A | 0005737 | cellular_component | cytoplasm |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005829 | cellular_component | cytosol |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0016020 | cellular_component | membrane |
A | 0016301 | molecular_function | kinase activity |
A | 0016525 | biological_process | negative regulation of angiogenesis |
A | 0030855 | biological_process | epithelial cell differentiation |
A | 0031639 | biological_process | plasminogen activation |
A | 0043531 | molecular_function | ADP binding |
A | 0045121 | cellular_component | membrane raft |
A | 0047134 | molecular_function | protein-disulfide reductase (NAD(P)H) activity |
A | 0061621 | biological_process | canonical glycolysis |
A | 0070062 | cellular_component | extracellular exosome |
A | 0071456 | biological_process | cellular response to hypoxia |
A | 0160218 | ||
B | 0004618 | molecular_function | phosphoglycerate kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005615 | cellular_component | extracellular space |
B | 0005737 | cellular_component | cytoplasm |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005829 | cellular_component | cytosol |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0016020 | cellular_component | membrane |
B | 0016301 | molecular_function | kinase activity |
B | 0016525 | biological_process | negative regulation of angiogenesis |
B | 0030855 | biological_process | epithelial cell differentiation |
B | 0031639 | biological_process | plasminogen activation |
B | 0043531 | molecular_function | ADP binding |
B | 0045121 | cellular_component | membrane raft |
B | 0047134 | molecular_function | protein-disulfide reductase (NAD(P)H) activity |
B | 0061621 | biological_process | canonical glycolysis |
B | 0070062 | cellular_component | extracellular exosome |
B | 0071456 | biological_process | cellular response to hypoxia |
B | 0160218 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG B 417 |
Chain | Residue |
B | ASP218 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 3PG B 418 |
Chain | Residue |
B | ARG170 |
B | ASP23 |
B | ASN25 |
B | ARG38 |
B | HIS62 |
B | ARG65 |
B | ARG122 |
B | GLY166 |
B | THR167 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 3PG A 417 |
Chain | Residue |
A | ASP23 |
A | ASN25 |
A | ARG38 |
A | HIS62 |
A | ARG65 |
A | ARG122 |
A | GLY166 |
A | ARG170 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ADP B 419 |
Chain | Residue |
B | GLY213 |
B | ALA214 |
B | ASP218 |
B | LYS219 |
B | GLY237 |
B | GLY238 |
B | GLY312 |
B | PRO338 |
B | GLY340 |
B | GLU343 |
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 | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18463139 |
Chain | Residue | Details |
A | ASP23 | |
B | ASP23 | |
B | ARG38 | |
B | HIS62 | |
B | ARG122 | |
B | ARG170 | |
B | LYS219 | |
B | GLY312 | |
B | GLU343 | |
B | GLY372 | |
A | ARG38 | |
A | HIS62 | |
A | ARG122 | |
A | ARG170 | |
A | LYS219 | |
A | GLY312 | |
A | GLU343 | |
A | GLY372 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER1 | |
A | SER3 | |
B | SER1 | |
B | SER3 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P09411 |
Chain | Residue | Details |
A | LYS5 | |
A | LYS190 | |
B | LYS5 | |
B | LYS190 |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS10 | |
B | LYS85 | |
B | LYS145 | |
B | LYS198 | |
B | LYS266 | |
B | LYS290 | |
A | LYS74 | |
A | LYS85 | |
A | LYS145 | |
A | LYS198 | |
A | LYS266 | |
A | LYS290 | |
B | LYS10 | |
B | LYS74 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09411 |
Chain | Residue | Details |
A | LYS47 | |
B | LYS47 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09411 |
Chain | Residue | Details |
A | TYR75 | |
B | TYR75 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09411 |
Chain | Residue | Details |
A | LYS90 | |
A | LYS360 | |
B | LYS90 | |
B | LYS360 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS96 | |
B | LYS96 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 |
Chain | Residue | Details |
A | LYS130 | |
B | LYS130 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
Chain | Residue | Details |
A | TYR195 | |
B | TYR195 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER202 | |
B | SER202 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581 |
Chain | Residue | Details |
A | LYS215 | |
A | LYS322 | |
B | LYS215 | |
B | LYS322 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 |
Chain | Residue | Details |
A | LYS219 | |
B | LYS219 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 13pk |
Chain | Residue | Details |
A | ARG38 | |
A | LYS215 | |
A | GLY396 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 13pk |
Chain | Residue | Details |
B | ARG38 | |
B | LYS215 | |
B | GLY396 |