5VYT
Crystal structure of the WbkC N-formyltransferase (F142A 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 | 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 | 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 |
| 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 | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0071951 | biological_process | conversion of methionyl-tRNA to N-formyl-methionyl-tRNA |
| 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 | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0071951 | biological_process | conversion of methionyl-tRNA to N-formyl-methionyl-tRNA |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue FON A 301 |
| Chain | Residue |
| A | TYR87 |
| A | ASP143 |
| A | HOH412 |
| A | ARG88 |
| A | SER89 |
| A | LEU90 |
| A | ILE91 |
| A | ASN105 |
| A | ASP139 |
| A | ASN141 |
| A | ALA142 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue GDP A 302 |
| Chain | Residue |
| A | ARG45 |
| A | ARG88 |
| A | ASN118 |
| A | VAL120 |
| A | ALA161 |
| A | PHE165 |
| A | LEU203 |
| A | MET225 |
| A | PHE227 |
| A | PHE230 |
| A | PRO231 |
| A | HOH424 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue FON B 301 |
| Chain | Residue |
| B | TYR87 |
| B | ARG88 |
| B | SER89 |
| B | LEU90 |
| B | ILE91 |
| B | ASN105 |
| B | ASP139 |
| B | ASN141 |
| B | ALA142 |
| B | ASP143 |
| B | HOH414 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue GDP B 302 |
| Chain | Residue |
| B | ARG45 |
| B | ARG88 |
| B | ASN118 |
| B | ALA161 |
| B | LEU203 |
| B | MET225 |
| B | PHE227 |
| B | PHE230 |
| B | HOH416 |
| B | HOH440 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue FON C 301 |
| Chain | Residue |
| C | TYR87 |
| C | SER89 |
| C | LEU90 |
| C | ILE91 |
| C | ASN105 |
| C | MET138 |
| C | ASP139 |
| C | ASN141 |
| C | ALA142 |
| C | ASP143 |
| C | ARG201 |
| C | HOH410 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue GDP C 302 |
| Chain | Residue |
| C | ARG45 |
| C | ARG88 |
| C | ASN118 |
| C | VAL120 |
| C | ALA161 |
| C | PHE165 |
| C | LEU203 |
| C | MET225 |
| C | PHE227 |
| C | PHE230 |
| C | PRO231 |
| C | HOH401 |
| C | HOH435 |
| C | HOH438 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 303 |
| Chain | Residue |
| D | TRP213 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue FON D 301 |
| Chain | Residue |
| D | TYR87 |
| D | ARG88 |
| D | SER89 |
| D | LEU90 |
| D | ILE91 |
| D | LEU96 |
| D | ASN105 |
| D | MET138 |
| D | ASP143 |
| D | ARG201 |
| D | HOH412 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue GDP D 302 |
| Chain | Residue |
| D | ARG45 |
| D | ARG88 |
| D | ASN118 |
| D | MET225 |
| D | PHE230 |
| D | HOH405 |
| D | HOH408 |
| D | HOH420 |
| D | HOH438 |
| D | HOH447 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28636341","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
