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 |