8YHP
Structure of the PGK1 from Biortus.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004618 | molecular_function | phosphoglycerate 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 | 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 | 0016310 | biological_process | phosphorylation |
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 |
Functional Information from PROSITE/UniProt
site_id | PS00111 |
Number of Residues | 11 |
Details | PGLYCERATE_KINASE Phosphoglycerate kinase signature. RVVMRvDfNVP |
Chain | Residue | Details |
A | ARG18-PRO28 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18463139 |
Chain | Residue | Details |
A | ASP24 | |
A | ARG39 | |
A | HIS63 | |
A | ARG123 | |
A | ARG171 | |
A | LYS220 | |
A | GLY313 | |
A | GLU344 | |
A | GLY373 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER2 | |
A | SER4 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P09411 |
Chain | Residue | Details |
A | LYS6 | |
A | LYS191 |
site_id | SWS_FT_FI4 |
Number of Residues | 7 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS11 | |
A | LYS75 | |
A | LYS86 | |
A | LYS146 | |
A | LYS199 | |
A | LYS267 | |
A | LYS291 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09411 |
Chain | Residue | Details |
A | LYS48 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09411 |
Chain | Residue | Details |
A | TYR76 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09411 |
Chain | Residue | Details |
A | LYS91 | |
A | LYS361 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS97 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 |
Chain | Residue | Details |
A | LYS131 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
Chain | Residue | Details |
A | TYR196 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
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 | SER203 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581 |
Chain | Residue | Details |
A | LYS216 | |
A | LYS323 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 |
Chain | Residue | Details |
A | LYS220 |