2B99
Crystal Structure of an archaeal pentameric riboflavin synthase Complex with a Substrate analog inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004746 | molecular_function | riboflavin synthase activity |
| A | 0009231 | biological_process | riboflavin biosynthetic process |
| A | 0009349 | cellular_component | riboflavin synthase complex |
| A | 0016740 | molecular_function | transferase activity |
| B | 0004746 | molecular_function | riboflavin synthase activity |
| B | 0009231 | biological_process | riboflavin biosynthetic process |
| B | 0009349 | cellular_component | riboflavin synthase complex |
| B | 0016740 | molecular_function | transferase activity |
| C | 0004746 | molecular_function | riboflavin synthase activity |
| C | 0009231 | biological_process | riboflavin biosynthetic process |
| C | 0009349 | cellular_component | riboflavin synthase complex |
| C | 0016740 | molecular_function | transferase activity |
| D | 0004746 | molecular_function | riboflavin synthase activity |
| D | 0009231 | biological_process | riboflavin biosynthetic process |
| D | 0009349 | cellular_component | riboflavin synthase complex |
| D | 0016740 | molecular_function | transferase activity |
| E | 0004746 | molecular_function | riboflavin synthase activity |
| E | 0009231 | biological_process | riboflavin biosynthetic process |
| E | 0009349 | cellular_component | riboflavin synthase complex |
| E | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE RDL C 1201 |
| Chain | Residue |
| C | PHE12 |
| C | CYS76 |
| C | HOH1217 |
| E | ILE96 |
| E | GLU97 |
| E | HIS122 |
| E | RDL1202 |
| C | GLY41 |
| C | ILE42 |
| C | LYS43 |
| C | ASP44 |
| C | MET66 |
| C | PRO67 |
| C | GLY68 |
| C | ASP73 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE RDL E 1202 |
| Chain | Residue |
| C | PHE12 |
| C | ASP73 |
| C | RDL1201 |
| E | PHE99 |
| E | ARG118 |
| E | HIS122 |
| E | ARG145 |
| E | GLN146 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE RDL D 1203 |
| Chain | Residue |
| C | ILE96 |
| C | GLU97 |
| C | HIS122 |
| C | GLN146 |
| C | RDL1204 |
| D | PHE12 |
| D | PRO40 |
| D | GLY41 |
| D | ILE42 |
| D | LYS43 |
| D | ASP44 |
| D | MET66 |
| D | PRO67 |
| D | GLY68 |
| D | ASP73 |
| D | CYS76 |
| D | HOH1204 |
| D | HOH1208 |
| D | HOH1209 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RDL C 1204 |
| Chain | Residue |
| C | PHE99 |
| C | HIS101 |
| C | ARG118 |
| C | HIS122 |
| C | ARG145 |
| C | GLN146 |
| C | HOH1205 |
| D | ASP73 |
| D | RDL1203 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE RDL A 1205 |
| Chain | Residue |
| A | PHE12 |
| A | GLY41 |
| A | ILE42 |
| A | LYS43 |
| A | ASP44 |
| A | MET66 |
| A | PRO67 |
| A | GLY68 |
| A | ASP73 |
| A | CYS76 |
| A | HOH1223 |
| B | ILE96 |
| B | GLU97 |
| B | HIS122 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE RDL E 1207 |
| Chain | Residue |
| A | ILE96 |
| A | GLU97 |
| A | HIS122 |
| A | RDL1208 |
| E | PHE12 |
| E | GLY41 |
| E | ILE42 |
| E | LYS43 |
| E | ASP44 |
| E | MET66 |
| E | PRO67 |
| E | GLY68 |
| E | ASP73 |
| E | CYS76 |
| E | HOH1216 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE RDL A 1208 |
| Chain | Residue |
| A | PHE99 |
| A | GLU104 |
| A | ARG118 |
| A | HIS122 |
| A | ARG145 |
| E | PHE12 |
| E | ASP73 |
| E | RDL1207 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE RDL B 1209 |
| Chain | Residue |
| B | PHE12 |
| B | ASP73 |
| B | RDL1210 |
| D | PHE99 |
| D | GLU104 |
| D | ARG118 |
| D | HIS122 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE RDL B 1210 |
| Chain | Residue |
| B | ASP44 |
| B | MET66 |
| B | PRO67 |
| B | GLY68 |
| B | ASP73 |
| B | CYS76 |
| B | RDL1209 |
| B | HOH1222 |
| D | ILE96 |
| D | GLU97 |
| D | HIS122 |
| B | PHE12 |
| B | GLY41 |
| B | ILE42 |
| B | LYS43 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rvv |
| Chain | Residue | Details |
| A | LYS72 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rvv |
| Chain | Residue | Details |
| B | LYS72 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rvv |
| Chain | Residue | Details |
| C | LYS72 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rvv |
| Chain | Residue | Details |
| D | LYS72 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rvv |
| Chain | Residue | Details |
| E | LYS72 |
