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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 395 |
| Chain | Residue |
| A | ARG206 |
| A | ARG206 |
| A | PHE249 |
| A | PHE249 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 396 |
| Chain | Residue |
| A | GLY195 |
| A | ALA196 |
| A | GLY220 |
| A | HOH512 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 397 |
| Chain | Residue |
| A | LYS383 |
| A | GLU384 |
| A | LYS256 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 398 |
| Chain | Residue |
| A | GLY317 |
| A | GLY350 |
| A | ASP352 |
| A | SER353 |
| A | HOH678 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 399 |
| Chain | Residue |
| A | LYS180 |
| A | GLU186 |
| A | LEU312 |
| A | HOH446 |
| A | HOH449 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 400 |
| Chain | Residue |
| A | HOH403 |
| A | HOH404 |
| A | HOH405 |
| A | HOH406 |
| A | HOH407 |
| A | HOH408 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BTB A 401 |
| Chain | Residue |
| A | ARG187 |
| A | ASP210 |
| A | LYS211 |
| A | VAL212 |
| A | ASP213 |
| A | LYS256 |
| A | GLU384 |
| A | HOH523 |
| A | HOH562 |
| A | HOH567 |
| A | HOH712 |
Functional Information from PROSITE/UniProt
| site_id | PS00111 |
| Number of Residues | 11 |
| Details | PGLYCERATE_KINASE Phosphoglycerate kinase signature. RVFCRvDfNVP |
| Chain | Residue | Details |
| A | ARG15-PRO25 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00145","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"HAMAP-Rule","id":"MF_00145","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"HAMAP-Rule","id":"MF_00145","evidenceCode":"ECO:0000255"}]} |
3UWD
