4IQFFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004479 | molecular_function | methionyl-tRNA formyltransferase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006413 | biological_process | translational initiation |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0019988 | biological_process | charged-tRNA amino acid modification |
| A | 0071951 | biological_process | conversion of methionyl-tRNA to N-formyl-methionyl-tRNA |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004479 | molecular_function | methionyl-tRNA formyltransferase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006413 | biological_process | translational initiation |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0019988 | biological_process | charged-tRNA amino acid modification |
| B | 0071951 | biological_process | conversion of methionyl-tRNA to N-formyl-methionyl-tRNA |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004479 | molecular_function | methionyl-tRNA formyltransferase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006413 | biological_process | translational initiation |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0019988 | biological_process | charged-tRNA amino acid modification |
| C | 0071951 | biological_process | conversion of methionyl-tRNA to N-formyl-methionyl-tRNA |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004479 | molecular_function | methionyl-tRNA formyltransferase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006413 | biological_process | translational initiation |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0019988 | biological_process | charged-tRNA amino acid modification |
| D | 0071951 | biological_process | conversion of methionyl-tRNA to N-formyl-methionyl-tRNA |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG5 A 401 |
| Chain | Residue |
| A | TYR123 |
| A | MSE126 |
| A | GLU127 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 402 |
| Chain | Residue |
| A | HOH625 |
| A | ALA87 |
| A | HIS108 |
| A | ALA109 |
| A | PHE166 |
| A | HOH527 |
| A | HOH528 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | ARG159 |
| A | HOH549 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 401 |
| Chain | Residue |
| B | ALA87 |
| B | VAL107 |
| B | HIS108 |
| B | ALA109 |
| B | PRO120 |
| B | HOH508 |
| B | HOH523 |
| B | HOH524 |
| B | HOH551 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 402 |
| Chain | Residue |
| B | TYR123 |
| B | MSE126 |
| B | GLU127 |
| B | HOH548 |
| B | HOH622 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 401 |
| Chain | Residue |
| C | PHE12 |
| C | ALA87 |
| C | HIS108 |
| C | ALA109 |
| C | PRO120 |
| C | PHE166 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 401 |
| Chain | Residue |
| D | PHE12 |
| D | ALA87 |
| D | HIS108 |
| D | ALA109 |
| D | PRO120 |
| D | PHE166 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 402 |
| Chain | Residue |
| D | LYS129 |
| D | GLU130 |
| D | LYS131 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 403 |
| Chain | Residue |
| D | SER294 |
| D | SER296 |
| D | GLN297 |
| D | ARG300 |
Functional Information from PROSITE/UniProt
| site_id | PS00373 |
| Number of Residues | 24 |
| Details | GART Phosphoribosylglycinamide formyltransferase active site. GiTImYMvEkLDaGdiLtqveveI |
| Chain | Residue | Details |
| A | GLY133-ILE156 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00182","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
