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 |