6HVJ
Human PFKFB3 in complex with a N-Aryl 6-Aminoquinoxaline inhibitor 3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0008152 | biological_process | metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 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 |
| 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 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:22275052 |
| Chain | Residue | Details |
| A | HIS253 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:22275052 |
| Chain | Residue | Details |
| A | 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 |
| A | ASN163 | |
| A | TYR424 | |
| A | GLY41 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16316985 |
| Chain | Residue | Details |
| A | ARG98 | |
| A | THR126 | |
| A | ARG132 | |
| A | LYS168 | |
| A | ARG189 | |
| A | TYR193 | |
| A | ARG74 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25849762 |
| Chain | Residue | Details |
| A | GLN388 | |
| A | ARG252 | |
| A | ASN259 | |
| A | GLY265 | |
| A | TYR333 | |
| A | ARG347 | |
| A | LYS351 | |
| A | TYR362 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07953 |
| Chain | Residue | Details |
| A | ARG392 | |
| A | TYR344 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | SITE: Transition state stabilizer => ECO:0000269|PubMed:22275052 |
| Chain | Residue | Details |
| A | ASN259 | |
| A | HIS387 | |
| A | ARG252 |
| 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 |
| A | SER460 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | 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 |
| A | SER466 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000250 |
| Chain | Residue | Details |
| A | THR470 |
