5DAB
Crystal structure of FTO-IN115
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 | 5 |
Details | binding site for residue CL A 601 |
Chain | Residue |
A | LYS45 |
A | TYR46 |
A | PRO47 |
A | LYS48 |
A | LEU301 |
site_id | AC2 |
Number of Residues | 1 |
Details | binding site for residue CL A 602 |
Chain | Residue |
A | TRP278 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue CL A 604 |
Chain | Residue |
A | LEU406 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue CL A 606 |
Chain | Residue |
A | TYR199 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue CL A 608 |
Chain | Residue |
A | CYS249 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue FE2 A 610 |
Chain | Residue |
A | HIS231 |
A | HIS307 |
A | AKG611 |
A | HOH762 |
site_id | AC7 |
Number of Residues | 14 |
Details | binding site for residue AKG A 611 |
Chain | Residue |
A | ARG96 |
A | TYR108 |
A | ASN205 |
A | VAL228 |
A | VAL244 |
A | TYR295 |
A | VAL309 |
A | ARG316 |
A | SER318 |
A | THR320 |
A | FE2610 |
A | HOH719 |
A | HOH756 |
A | HOH762 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue 58W A 612 |
Chain | Residue |
A | TYR39 |
A | ILE85 |
A | LEU90 |
A | LEU91 |
A | THR92 |
A | PRO93 |
A | LEU215 |
A | LYS216 |
A | MET226 |
A | ALA227 |
A | SER229 |
A | HOH722 |
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 |