Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004618 | molecular_function | phosphoglycerate kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0016301 | molecular_function | kinase activity |
A | 0043531 | molecular_function | ADP binding |
B | 0004618 | molecular_function | phosphoglycerate kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0016301 | molecular_function | kinase activity |
B | 0043531 | molecular_function | ADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K A 401 |
Chain | Residue |
A | SER343 |
A | GLY345 |
A | GLU368 |
A | HOH427 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K A 402 |
Chain | Residue |
A | ALA136 |
A | VAL139 |
A | HOH447 |
A | HOH473 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT A 403 |
Chain | Residue |
A | PHE227 |
A | PRO267 |
A | ASP298 |
A | ILE299 |
A | MSE323 |
A | HOH494 |
A | GLY223 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 404 |
Chain | Residue |
A | ARG64 |
A | ARG119 |
A | GLY148 |
A | VAL149 |
A | HOH521 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PGE A 405 |
Chain | Residue |
A | ILE264 |
A | TYR265 |
A | LEU266 |
A | VAL268 |
A | LEU306 |
A | HOH481 |
B | TYR235 |
B | GLN288 |
B | HOH432 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K B 401 |
Chain | Residue |
B | SER343 |
B | GLY345 |
B | GLU368 |
B | HOH412 |
B | HOH501 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE K B 402 |
Chain | Residue |
B | ALA136 |
B | VAL139 |
B | HOH507 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT B 403 |
Chain | Residue |
B | ALA82 |
B | GLU88 |
B | ILE89 |
B | ASN259 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT B 404 |
Chain | Residue |
B | GLY223 |
B | ASP298 |
B | ILE299 |
B | MSE323 |
B | HOH479 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT B 405 |
Chain | Residue |
B | ILE264 |
B | HOH517 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 406 |
Chain | Residue |
B | HIS61 |
B | ARG64 |
B | ARG119 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PGE B 407 |
Chain | Residue |
B | LYS177 |
B | ASP180 |
Functional Information from PROSITE/UniProt
site_id | PS00111 |
Number of Residues | 11 |
Details | PGLYCERATE_KINASE Phosphoglycerate kinase signature. KVFIRcDfNVP |
Chain | Residue | Details |
A | LYS16-PRO26 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP22 | |
B | ASP22 | |
B | ARG38 | |
B | HIS61 | |
B | ARG119 | |
B | ARG152 | |
B | LYS205 | |
B | GLY296 | |
B | GLU327 | |
B | GLY353 | |
A | ARG38 | |
A | HIS61 | |
A | ARG119 | |
A | ARG152 | |
A | LYS205 | |
A | GLY296 | |
A | GLU327 | |
A | GLY353 | |