Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008703 | molecular_function | 5-amino-6-(5-phosphoribosylamino)uracil reductase activity |
A | 0009231 | biological_process | riboflavin biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0050661 | molecular_function | NADP binding |
B | 0008703 | molecular_function | 5-amino-6-(5-phosphoribosylamino)uracil reductase activity |
B | 0009231 | biological_process | riboflavin biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue CL A 301 |
Chain | Residue |
A | ARG39 |
A | ARG58 |
A | LEU59 |
A | HIS62 |
A | HOH489 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
A | GLU30 |
A | HIS136 |
A | GLU141 |
A | GLY205 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue GOL A 303 |
Chain | Residue |
A | ARG40 |
A | CYS42 |
A | ASP43 |
A | GLY69 |
A | ASP70 |
A | PRO72 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue GOL A 304 |
Chain | Residue |
A | ARG34 |
A | PRO95 |
A | THR96 |
A | VAL97 |
A | GLU117 |
A | ARG200 |
A | GLU211 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue GOL A 305 |
Chain | Residue |
A | ILE6 |
A | GLU117 |
A | GLU163 |
A | ARG165 |
A | HOH458 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG A 306 |
Chain | Residue |
A | ARG176 |
A | HOH447 |
A | HOH464 |
B | ARG176 |
B | HOH414 |
B | HOH433 |
site_id | AC7 |
Number of Residues | 25 |
Details | binding site for residue NAP A 307 |
Chain | Residue |
A | ALA9 |
A | ALA10 |
A | ILE17 |
A | GLY48 |
A | ILE49 |
A | ASN50 |
A | THR51 |
A | ASP55 |
A | VAL77 |
A | SER79 |
A | ARG82 |
A | ARG125 |
A | VAL126 |
A | LEU128 |
A | GLU146 |
A | GLY148 |
A | SER149 |
A | THR150 |
A | LEU151 |
A | SER154 |
A | ARG179 |
A | HOH408 |
A | HOH436 |
A | HOH450 |
A | HOH484 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue CL B 301 |
Chain | Residue |
B | ARG39 |
B | ARG58 |
B | LEU59 |
B | HOH474 |
site_id | AC9 |
Number of Residues | 23 |
Details | binding site for residue NAP B 302 |
Chain | Residue |
B | ALA9 |
B | ALA10 |
B | ILE17 |
B | GLY48 |
B | ILE49 |
B | ASN50 |
B | THR51 |
B | ASP55 |
B | VAL77 |
B | SER79 |
B | ARG82 |
B | ARG125 |
B | VAL126 |
B | LEU128 |
B | GLU146 |
B | GLY148 |
B | SER149 |
B | THR150 |
B | LEU151 |
B | SER154 |
B | ARG179 |
B | HOH423 |
B | HOH431 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY148 | |
B | THR51 | |
B | ASP55 | |
B | SER79 | |
B | VAL126 | |
B | GLY148 | |
A | THR51 | |
A | ASP55 | |
A | SER79 | |
A | VAL126 | |