Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009058 | biological_process | biosynthetic process |
B | 0009058 | biological_process | biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue 0FX A 301 |
Chain | Residue |
A | ASN21 |
A | PHE232 |
A | ASN234 |
A | HOH403 |
A | HOH411 |
A | HOH413 |
A | HOH433 |
A | HOH466 |
A | HIS87 |
A | LYS89 |
A | TRP116 |
A | TYR117 |
A | GLN119 |
A | TYR163 |
A | TYR203 |
A | HIS229 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue FOL A 302 |
Chain | Residue |
A | SER85 |
A | CYS88 |
A | LYS89 |
A | GLN90 |
A | LEU91 |
A | PHE92 |
A | ASN104 |
A | HIS134 |
A | MET136 |
A | ASP137 |
A | GLU138 |
A | ALA139 |
A | ASP141 |
A | HOH408 |
A | HOH429 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | SER155 |
A | ARG218 |
A | ILE221 |
A | ASN222 |
A | ARG225 |
B | LEU211 |
site_id | AC4 |
Number of Residues | 17 |
Details | binding site for residue 0FX B 301 |
Chain | Residue |
B | ASN21 |
B | HIS87 |
B | LYS89 |
B | TRP116 |
B | TYR117 |
B | GLN119 |
B | TYR163 |
B | TYR203 |
B | HIS229 |
B | PHE232 |
B | ASN234 |
B | HOH404 |
B | HOH425 |
B | HOH431 |
B | HOH434 |
B | HOH439 |
B | HOH448 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue FOL B 302 |
Chain | Residue |
B | SER85 |
B | CYS88 |
B | LYS89 |
B | GLN90 |
B | LEU91 |
B | PHE92 |
B | ASN104 |
B | TRP116 |
B | HIS134 |
B | MET136 |
B | ASP137 |
B | ALA139 |
B | ASP141 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
A | LEU211 |
B | SER155 |
B | ASN222 |
B | ARG225 |
Functional Information from PROSITE/UniProt
site_id | PS00373 |
Number of Residues | 24 |
Details | GART Phosphoribosylglycinamide formyltransferase active site. GaTIhVMdEaIDhGhiIvqrqveV |
Chain | Residue | Details |
A | GLY130-VAL153 | |