4G3M
Complex Structure of Bacillus subtilis RibG: The Deamination Process 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS49 |
| A | GLU51 |
| A | CYS74 |
| A | CYS83 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AI9 A 402 |
| Chain | Residue |
| A | ARG176 |
| A | ARG183 |
| A | ASP199 |
| A | PRO201 |
| A | SER202 |
| A | LEU203 |
| A | THR204 |
| A | ARG206 |
| A | GLU290 |
| A | HOH511 |
| A | HOH546 |
| A | HOH603 |
| A | LYS151 |
| A | ALA153 |
| A | SER167 |
| A | ILE170 |
| A | THR171 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS49 |
| B | CYS74 |
| B | CYS83 |
| B | AOF402 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AOF B 402 |
| Chain | Residue |
| B | ASN23 |
| B | VAL26 |
| B | HIS42 |
| B | HIS49 |
| B | ALA50 |
| B | GLU51 |
| B | CYS74 |
| B | HIS76 |
| B | LYS79 |
| B | THR80 |
| B | CYS83 |
| B | ASP101 |
| B | ASN103 |
| B | PHE137 |
| B | ZN401 |
| B | HOH503 |
| B | HOH533 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AI9 B 403 |
| Chain | Residue |
| B | LYS151 |
| B | ALA153 |
| B | SER167 |
| B | ILE170 |
| B | THR171 |
| B | ARG176 |
| B | ARG183 |
| B | ASP199 |
| B | PRO201 |
| B | SER202 |
| B | LEU203 |
| B | ARG206 |
| B | HOH568 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 401 |
| Chain | Residue |
| C | HIS49 |
| C | CYS74 |
| C | CYS83 |
| C | AOF402 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AOF C 402 |
| Chain | Residue |
| C | ASN23 |
| C | PRO24 |
| C | VAL26 |
| C | HIS42 |
| C | HIS49 |
| C | ALA50 |
| C | GLU51 |
| C | CYS74 |
| C | GLY78 |
| C | LYS79 |
| C | THR80 |
| C | ASP101 |
| C | PHE137 |
| C | ZN401 |
| C | HOH550 |
| C | HOH561 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AI9 C 403 |
| Chain | Residue |
| C | LYS151 |
| C | ALA153 |
| C | SER167 |
| C | TRP169 |
| C | ILE170 |
| C | THR171 |
| C | ARG176 |
| C | ARG183 |
| C | ASP199 |
| C | PRO201 |
| C | SER202 |
| C | LEU203 |
| C | ARG206 |
| C | GLU290 |
| C | HOH506 |
| C | HOH549 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 401 |
| Chain | Residue |
| D | HIS49 |
| D | CYS74 |
| D | CYS83 |
| D | AOF402 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AOF D 402 |
| Chain | Residue |
| D | HIS49 |
| D | ALA50 |
| D | GLU51 |
| D | CYS74 |
| D | HIS76 |
| D | GLY78 |
| D | LYS79 |
| D | THR80 |
| D | CYS83 |
| D | ASP101 |
| D | PHE137 |
| D | ZN401 |
| D | HOH530 |
| D | HOH549 |
| D | ASN23 |
| D | PRO24 |
| D | VAL26 |
| D | HIS42 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AI9 D 403 |
| Chain | Residue |
| D | LYS151 |
| D | ALA153 |
| D | ILE170 |
| D | THR171 |
| D | ARG176 |
| D | ARG183 |
| D | ASP199 |
| D | PRO201 |
| D | SER202 |
| D | LEU203 |
| D | ARG206 |
| D | GLU290 |
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 |
