Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0003873 | molecular_function | 6-phosphofructo-2-kinase activity |
A | 0004331 | molecular_function | fructose-2,6-bisphosphate 2-phosphatase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006000 | biological_process | fructose metabolic process |
A | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
A | 0006096 | biological_process | glycolytic process |
A | 0006915 | biological_process | apoptotic process |
A | 0010001 | biological_process | glial cell differentiation |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046835 | biological_process | carbohydrate phosphorylation |
A | 0061744 | biological_process | motor behavior |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE POP A 520 |
Chain | Residue |
A | GLY71 |
A | HOH595 |
A | HOH693 |
A | EDO750 |
A | ARG74 |
A | PHE87 |
A | ARG98 |
A | ALA125 |
A | THR126 |
A | TYR193 |
A | HOH553 |
A | HOH560 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE POP A 550 |
Chain | Residue |
A | PRO43 |
A | ALA44 |
A | ARG45 |
A | GLY46 |
A | LYS47 |
A | THR48 |
A | TYR49 |
A | VAL167 |
A | LYS168 |
A | TYR424 |
A | HOH620 |
A | HOH622 |
A | EDO750 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE POP A 600 |
Chain | Residue |
A | ARG252 |
A | HIS253 |
A | ASN256 |
A | ASN259 |
A | GLY265 |
A | GLU322 |
A | HIS387 |
A | GLN388 |
A | HOH578 |
A | HOH691 |
A | HOH734 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SRT A 650 |
Chain | Residue |
A | TYR333 |
A | ARG347 |
A | LYS351 |
A | GLN388 |
A | ARG392 |
A | HIS441 |
A | ARG442 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SRT A 700 |
Chain | Residue |
A | GLN227 |
A | ASP228 |
A | HIS229 |
A | ARG294 |
A | GLU375 |
A | ARG378 |
A | GLN379 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 750 |
Chain | Residue |
A | THR48 |
A | ASN69 |
A | ASP124 |
A | ALA125 |
A | POP520 |
A | POP550 |
A | HOH620 |
A | HOH707 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 800 |
Chain | Residue |
A | PHE87 |
A | PRO89 |
A | ARG98 |
A | CYS192 |
Functional Information from PROSITE/UniProt
site_id | PS00175 |
Number of Residues | 10 |
Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEnEhN |
Chain | Residue | Details |
A | LEU250-ASN259 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000255 |
Chain | Residue | Details |
A | ASP124 | |
A | CYS154 | |
Chain | Residue | Details |
A | HIS253 | |
Chain | Residue | Details |
A | GLU322 | |
Chain | Residue | Details |
A | GLY41 | |
A | ASN163 | |
A | TYR424 | |
Chain | Residue | Details |
A | ARG74 | |
A | ARG98 | |
A | THR126 | |
A | ARG132 | |
A | LYS168 | |
A | ARG189 | |
A | TYR193 | |
Chain | Residue | Details |
A | ARG252 | |
A | ASN259 | |
A | GLY265 | |
A | TYR333 | |
A | ARG347 | |
A | LYS351 | |
A | TYR362 | |
A | GLN388 | |
Chain | Residue | Details |
A | TYR344 | |
A | ARG392 | |
Chain | Residue | Details |
A | ARG252 | |
A | ASN259 | |
A | HIS387 | |
Chain | Residue | Details |
A | SER460 | |
Chain | Residue | Details |
A | THR462 | |
Chain | Residue | Details |
A | SER466 | |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000250 |
Chain | Residue | Details |
A | THR470 | |