3EX8
Complex structure of bacillus subtilis RibG reduction mechanism in riboflavin biosynthesis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008703 | molecular_function | 5-amino-6-(5-phosphoribosylamino)uracil reductase activity |
A | 0008835 | molecular_function | diaminohydroxyphosphoribosylaminopyrimidine deaminase activity |
A | 0009231 | biological_process | riboflavin biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050661 | molecular_function | NADP binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008703 | molecular_function | 5-amino-6-(5-phosphoribosylamino)uracil reductase activity |
B | 0008835 | molecular_function | diaminohydroxyphosphoribosylaminopyrimidine deaminase activity |
B | 0009231 | biological_process | riboflavin biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050661 | molecular_function | NADP binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0008270 | molecular_function | zinc ion binding |
C | 0008703 | molecular_function | 5-amino-6-(5-phosphoribosylamino)uracil reductase activity |
C | 0008835 | molecular_function | diaminohydroxyphosphoribosylaminopyrimidine deaminase activity |
C | 0009231 | biological_process | riboflavin biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0050661 | molecular_function | NADP binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0008270 | molecular_function | zinc ion binding |
D | 0008703 | molecular_function | 5-amino-6-(5-phosphoribosylamino)uracil reductase activity |
D | 0008835 | molecular_function | diaminohydroxyphosphoribosylaminopyrimidine deaminase activity |
D | 0009231 | biological_process | riboflavin biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 362 |
Chain | Residue |
A | HIS49 |
A | CYS74 |
A | CYS83 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 362 |
Chain | Residue |
B | HIS49 |
B | GLU51 |
B | CYS74 |
B | CYS83 |
B | HOH400 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 362 |
Chain | Residue |
C | CYS74 |
C | CYS83 |
C | HOH383 |
C | HIS49 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AIF C 381 |
Chain | Residue |
C | LYS151 |
C | ALA153 |
C | SER167 |
C | TRP169 |
C | ILE170 |
C | THR171 |
C | ARG176 |
C | ARG183 |
C | THR195 |
C | ASP199 |
C | PRO201 |
C | SER202 |
C | LEU203 |
C | ARG206 |
C | GLU290 |
C | HOH382 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN D 362 |
Chain | Residue |
D | HIS49 |
D | CYS74 |
D | CYS83 |
Functional Information from PROSITE/UniProt
site_id | PS00903 |
Number of Residues | 39 |
Details | CYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAEvhAIhmagahaegadiyvtle................PCshygktppCaelI |
Chain | Residue | Details |
A | HIS49-ILE87 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | GLU51 | |
B | GLU51 | |
C | GLU51 | |
D | GLU51 |
site_id | SWS_FT_FI2 |
Number of Residues | 36 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS49 | |
B | HIS49 | |
B | CYS74 | |
B | CYS83 | |
B | ALA153 | |
B | TRP169 | |
B | THR195 | |
B | ASP199 | |
B | THR221 | |
B | GLY292 | |
C | HIS49 | |
A | CYS74 | |
C | CYS74 | |
C | CYS83 | |
C | ALA153 | |
C | TRP169 | |
C | THR195 | |
C | ASP199 | |
C | THR221 | |
C | GLY292 | |
D | HIS49 | |
D | CYS74 | |
A | CYS83 | |
D | CYS83 | |
D | ALA153 | |
D | TRP169 | |
D | THR195 | |
D | ASP199 | |
D | THR221 | |
D | GLY292 | |
A | ALA153 | |
A | TRP169 | |
A | THR195 | |
A | ASP199 | |
A | THR221 | |
A | GLY292 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER167 | |
B | GLU290 | |
C | SER167 | |
C | ARG183 | |
C | LEU203 | |
C | ARG206 | |
C | GLU290 | |
D | SER167 | |
D | ARG183 | |
D | LEU203 | |
D | ARG206 | |
A | ARG183 | |
D | GLU290 | |
A | LEU203 | |
A | ARG206 | |
A | GLU290 | |
B | SER167 | |
B | ARG183 | |
B | LEU203 | |
B | ARG206 |