5VYS
Crystal structure of the WbkC N-formyltransferase (C47S variant) from Brucella melitensis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004479 | molecular_function | methionyl-tRNA formyltransferase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006413 | biological_process | translational initiation |
| A | 0008446 | molecular_function | GDP-mannose 4,6-dehydratase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0071951 | biological_process | conversion of methionyl-tRNA to N-formyl-methionyl-tRNA |
| B | 0004479 | molecular_function | methionyl-tRNA formyltransferase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006413 | biological_process | translational initiation |
| B | 0008446 | molecular_function | GDP-mannose 4,6-dehydratase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0071951 | biological_process | conversion of methionyl-tRNA to N-formyl-methionyl-tRNA |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue 1YJ A 301 |
| Chain | Residue |
| A | TYR87 |
| A | ASP143 |
| A | HOH401 |
| A | HOH441 |
| A | SER89 |
| A | LEU90 |
| A | ILE91 |
| A | ASN105 |
| A | HIS136 |
| A | ASP139 |
| A | ASN141 |
| A | PHE142 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | GLU128 |
| A | GLU156 |
| A | GLU157 |
| A | ARG220 |
| A | ARG223 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue GDP A 303 |
| Chain | Residue |
| A | ARG45 |
| A | ARG88 |
| A | THR117 |
| A | ASN118 |
| A | VAL120 |
| A | ALA121 |
| A | ALA161 |
| A | ARG201 |
| A | MET225 |
| A | PHE227 |
| A | PHE230 |
| A | PRO231 |
| A | HOH415 |
| A | HOH445 |
| A | HOH472 |
| A | HOH480 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue 1YJ B 301 |
| Chain | Residue |
| B | SER89 |
| B | ILE91 |
| B | LEU96 |
| B | ASN105 |
| B | HIS136 |
| B | MET138 |
| B | ASP139 |
| B | ASN141 |
| B | PHE142 |
| B | ASP143 |
| B | HOH408 |
| B | HOH417 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue GDP B 302 |
| Chain | Residue |
| B | ARG45 |
| B | ARG88 |
| B | ASN118 |
| B | ALA161 |
| B | PHE165 |
| B | LEU203 |
| B | MET225 |
| B | PHE227 |
| B | PHE230 |
| B | PRO231 |
| B | HOH402 |
| B | HOH432 |
| B | HOH443 |
| B | HOH479 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue GMP B 303 |
| Chain | Residue |
| A | ARG212 |
| B | ARG88 |
| B | SER89 |
| B | GLY116 |
| B | THR117 |
| B | PHE142 |
| B | ASP143 |
| B | ARG201 |
| B | HOH406 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:28636341 |
| Chain | Residue | Details |
| A | SER89 | |
| A | ASP139 | |
| B | SER89 | |
| B | ASP139 |
