5VYU
Crystal structure of the WbkC N-formyltransferase from Brucella melitensis in complex with GDP-perosaminea and N-10-formyltetrahydrofolate
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 | 18 |
| Details | binding site for residue 1YA A 301 |
| Chain | Residue |
| A | TYR87 |
| A | GLU140 |
| A | ASN141 |
| A | ALA142 |
| A | ASP143 |
| A | JB2302 |
| A | HOH418 |
| A | HOH442 |
| A | HOH448 |
| B | ARG212 |
| A | ARG88 |
| A | SER89 |
| A | LEU90 |
| A | ILE91 |
| A | ASN105 |
| A | HIS136 |
| A | MET138 |
| A | ASP139 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue JB2 A 302 |
| Chain | Residue |
| A | ARG45 |
| A | ARG88 |
| A | GLY116 |
| A | THR117 |
| A | ASN118 |
| A | VAL120 |
| A | PHE165 |
| A | LEU203 |
| A | MET225 |
| A | PHE227 |
| A | PHE230 |
| A | PRO231 |
| A | 1YA301 |
| A | HOH406 |
| A | HOH412 |
| A | HOH443 |
| A | HOH445 |
| A | HOH446 |
| A | HOH478 |
| B | ARG212 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue 1YA B 301 |
| Chain | Residue |
| B | ARG88 |
| B | SER89 |
| B | LEU90 |
| B | ILE91 |
| B | ASN105 |
| B | HIS136 |
| B | MET138 |
| B | ASP139 |
| B | GLU140 |
| B | ASN141 |
| B | ALA142 |
| B | ASP143 |
| B | ARG201 |
| B | HOH416 |
| B | HOH441 |
| B | HOH468 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue GDP B 302 |
| Chain | Residue |
| B | ARG88 |
| B | THR117 |
| B | ASN118 |
| B | LEU203 |
| B | MET225 |
| B | PHE227 |
| B | PHE230 |
| B | PRO231 |
| 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 |
