2I1V
Crystal structure of PFKFB3 in complex with ADP and Fructose-2,6-bisphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003873 | molecular_function | 6-phosphofructo-2-kinase activity |
| B | 0004331 | molecular_function | fructose-2,6-bisphosphate 2-phosphatase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006000 | biological_process | fructose metabolic process |
| B | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00175 |
| Number of Residues | 10 |
| Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEnEhN |
| Chain | Residue | Details |
| B | 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 |
| B | ASP124 | |
| B | CYS154 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:22275052 |
| Chain | Residue | Details |
| B | HIS253 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:22275052 |
| Chain | Residue | Details |
| B | GLU322 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16316985, ECO:0000269|PubMed:17499765, ECO:0000269|PubMed:22275052 |
| Chain | Residue | Details |
| B | GLY41 | |
| B | ASN163 | |
| B | TYR424 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16316985 |
| Chain | Residue | Details |
| B | ARG74 | |
| B | ARG98 | |
| B | THR126 | |
| B | ARG132 | |
| B | LYS168 | |
| B | ARG189 | |
| B | TYR193 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25849762 |
| Chain | Residue | Details |
| B | ARG252 | |
| B | ASN259 | |
| B | GLY265 | |
| B | TYR333 | |
| B | ARG347 | |
| B | LYS351 | |
| B | TYR362 | |
| B | GLN388 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07953 |
| Chain | Residue | Details |
| B | TYR344 | |
| B | ARG392 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | SITE: Transition state stabilizer => ECO:0000269|PubMed:22275052 |
| Chain | Residue | Details |
| B | ARG252 | |
| B | ASN259 | |
| B | HIS387 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by AMPK => ECO:0000269|PubMed:12065600, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| B | SER460 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| B | THR462 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| B | SER466 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000250 |
| Chain | Residue | Details |
| B | THR470 |
