4QKN
Crystal structure of FTO bound to a selective inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001659 | biological_process | temperature homeostasis |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006307 | biological_process | DNA alkylation repair |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0010883 | biological_process | regulation of lipid storage |
| A | 0016180 | biological_process | snRNA processing |
| A | 0016607 | cellular_component | nuclear speck |
| A | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0035515 | molecular_function | oxidative RNA demethylase activity |
| A | 0035516 | molecular_function | broad specificity oxidative DNA demethylase activity |
| A | 0040014 | biological_process | regulation of multicellular organism growth |
| A | 0042245 | biological_process | RNA repair |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0044065 | biological_process | regulation of respiratory system process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0060612 | biological_process | adipose tissue development |
| A | 0061157 | biological_process | mRNA destabilization |
| A | 0070350 | biological_process | regulation of white fat cell proliferation |
| A | 0090335 | biological_process | regulation of brown fat cell differentiation |
| A | 1990931 | molecular_function | mRNA N6-methyladenosine dioxygenase activity |
| A | 1990984 | molecular_function | tRNA demethylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE OGA A 601 |
| Chain | Residue |
| A | ARG96 |
| A | SER318 |
| A | THR320 |
| A | ARG322 |
| A | MN603 |
| A | GOL604 |
| A | HOH767 |
| A | ASN205 |
| A | HIS231 |
| A | ASP233 |
| A | VAL244 |
| A | TYR295 |
| A | HIS307 |
| A | VAL309 |
| A | ARG316 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE JMS A 602 |
| Chain | Residue |
| A | LEU90 |
| A | ARG96 |
| A | LEU109 |
| A | VAL228 |
| A | SER229 |
| A | HIS231 |
| A | GOL604 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 603 |
| Chain | Residue |
| A | HIS231 |
| A | ASP233 |
| A | HIS307 |
| A | OGA601 |
| A | HOH767 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 604 |
| Chain | Residue |
| A | ARG96 |
| A | TYR106 |
| A | TYR108 |
| A | HIS232 |
| A | ASP233 |
| A | GLU234 |
| A | ARG322 |
| A | OGA601 |
| A | JMS602 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0007744|PDB:3LFM |
| Chain | Residue | Details |
| A | ARG96 | |
| A | TYR108 | |
| A | THR320 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0000269|PubMed:25452335, ECO:0007744|PDB:3LFM, ECO:0007744|PDB:4QKN |
| Chain | Residue | Details |
| A | ASN205 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0000269|PubMed:25452335, ECO:0000305|PubMed:23547775, ECO:0000305|PubMed:25452335, ECO:0000305|PubMed:26457839, ECO:0000305|PubMed:28553460, ECO:0007744|PDB:3LFM, ECO:0007744|PDB:4CXW, ECO:0007744|PDB:4CXX, ECO:0007744|PDB:4CXY, ECO:0007744|PDB:4IDZ, ECO:0007744|PDB:4IE0, ECO:0007744|PDB:4IE4, ECO:0007744|PDB:4IE5, ECO:0007744|PDB:4IE6, ECO:0007744|PDB:4IE7, ECO:0007744|PDB:4QKN, ECO:0007744|PDB:4ZS2, ECO:0007744|PDB:4ZS3 |
| Chain | Residue | Details |
| A | HIS231 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0000305|PubMed:23547775, ECO:0000305|PubMed:25452335, ECO:0000305|PubMed:26457839, ECO:0000305|PubMed:28553460, ECO:0007744|PDB:3LFM, ECO:0007744|PDB:4CXW, ECO:0007744|PDB:4CXX, ECO:0007744|PDB:4CXY, ECO:0007744|PDB:4IDZ, ECO:0007744|PDB:4IE0, ECO:0007744|PDB:4IE4, ECO:0007744|PDB:4IE5, ECO:0007744|PDB:4IE6, ECO:0007744|PDB:4IE7, ECO:0007744|PDB:4QKN, ECO:0007744|PDB:4ZS2, ECO:0007744|PDB:4ZS3 |
| Chain | Residue | Details |
| A | ASP233 | |
| A | HIS307 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0000269|PubMed:25452335, ECO:0000269|PubMed:26457839, ECO:0007744|PDB:3LFM, ECO:0007744|PDB:4QKN, ECO:0007744|PDB:4ZS2, ECO:0007744|PDB:4ZS3 |
| Chain | Residue | Details |
| A | TYR295 | |
| A | ARG316 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0000269|PubMed:25452335, ECO:0000269|PubMed:26457839, ECO:0007744|PDB:3LFM, ECO:0007744|PDB:4QKN, ECO:0007744|PDB:4ZS2 |
| Chain | Residue | Details |
| A | ARG322 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS216 |
