5VYR
Crystal structure of the WbkC formyl transferase 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 | 16 |
Details | binding site for residue B62 A 301 |
Chain | Residue |
A | TYR87 |
A | ASN141 |
A | PHE142 |
A | ASP143 |
A | HOH409 |
A | HOH457 |
A | HOH463 |
A | HOH482 |
A | SER89 |
A | LEU90 |
A | ILE91 |
A | LEU96 |
A | ASN105 |
A | HIS136 |
A | MET138 |
A | ASP139 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | GLU128 |
A | VAL155 |
A | GLU156 |
A | GLU157 |
A | ARG220 |
A | ARG223 |
A | HOH415 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CL A 303 |
Chain | Residue |
A | LEU110 |
A | THR131 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue GMP A 304 |
Chain | Residue |
A | MET225 |
A | PHE227 |
A | PHE230 |
A | PRO231 |
A | HOH407 |
A | HOH439 |
site_id | AC5 |
Number of Residues | 14 |
Details | binding site for residue B62 B 301 |
Chain | Residue |
B | SER89 |
B | LEU90 |
B | ILE91 |
B | ASN105 |
B | HIS136 |
B | MET138 |
B | ASP139 |
B | ASN141 |
B | PHE142 |
B | ASP143 |
B | HOH415 |
B | HOH433 |
B | HOH457 |
B | HOH476 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue GMP B 302 |
Chain | Residue |
A | ARG212 |
B | ARG88 |
B | GLY116 |
B | THR117 |
B | PHE142 |
B | ASP143 |
B | ARG201 |
B | HOH471 |
B | HOH511 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue GMP B 303 |
Chain | Residue |
B | LEU203 |
B | MET225 |
B | PHE230 |
B | PRO231 |
B | HOH477 |
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 |