1DI0
CRYSTAL STRUCTURE OF LUMAZINE SYNTHASE FROM BRUCELLA ABORTUS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000906 | molecular_function | 6,7-dimethyl-8-ribityllumazine synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0009231 | biological_process | riboflavin biosynthetic process |
| A | 0009349 | cellular_component | riboflavin synthase complex |
| A | 0016740 | molecular_function | transferase activity |
| B | 0000906 | molecular_function | 6,7-dimethyl-8-ribityllumazine synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0009231 | biological_process | riboflavin biosynthetic process |
| B | 0009349 | cellular_component | riboflavin synthase complex |
| B | 0016740 | molecular_function | transferase activity |
| C | 0000906 | molecular_function | 6,7-dimethyl-8-ribityllumazine synthase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0009231 | biological_process | riboflavin biosynthetic process |
| C | 0009349 | cellular_component | riboflavin synthase complex |
| C | 0016740 | molecular_function | transferase activity |
| D | 0000906 | molecular_function | 6,7-dimethyl-8-ribityllumazine synthase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0009231 | biological_process | riboflavin biosynthetic process |
| D | 0009349 | cellular_component | riboflavin synthase complex |
| D | 0016740 | molecular_function | transferase activity |
| E | 0000906 | molecular_function | 6,7-dimethyl-8-ribityllumazine synthase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 190 |
| Chain | Residue |
| A | GLY55 |
| A | ALA56 |
| A | TYR57 |
| A | GLU58 |
| A | VAL92 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 191 |
| Chain | Residue |
| A | HIS89 |
| A | HOH2014 |
| E | LYS135 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 192 |
| Chain | Residue |
| A | GLY85 |
| A | ILE86 |
| A | TYR87 |
| A | HIS89 |
| A | HOH2026 |
| C | HIS121 |
| C | HIS124 |
| A | GLY84 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 193 |
| Chain | Residue |
| B | GLY55 |
| B | ALA56 |
| B | TYR57 |
| B | PO4194 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 194 |
| Chain | Residue |
| A | LYS135 |
| B | HIS89 |
| B | PO4193 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 195 |
| Chain | Residue |
| B | GLY84 |
| B | GLY85 |
| B | ILE86 |
| B | TYR87 |
| B | HIS89 |
| B | HIS121 |
| B | HIS124 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 196 |
| Chain | Residue |
| C | GLY55 |
| C | ALA56 |
| C | TYR57 |
| C | GLU58 |
| C | HOH2016 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 C 197 |
| Chain | Residue |
| A | HIS121 |
| A | HIS124 |
| C | GLY84 |
| C | GLY85 |
| C | ILE86 |
| C | TYR87 |
| C | HIS89 |
| C | HOH2031 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 D 198 |
| Chain | Residue |
| D | GLY55 |
| D | ALA56 |
| D | TYR57 |
| D | GLU58 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 D 199 |
| Chain | Residue |
| D | GLY84 |
| D | GLY85 |
| D | ILE86 |
| D | TYR87 |
| D | HIS89 |
| E | HIS124 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 E 200 |
| Chain | Residue |
| E | GLY55 |
| E | ALA56 |
| E | TYR57 |
| E | GLU58 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 E 201 |
| Chain | Residue |
| D | LYS135 |
| E | HIS89 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 E 202 |
| Chain | Residue |
| D | HIS124 |
| E | GLY84 |
| E | GLY85 |
| E | ILE86 |
| E | TYR87 |
| E | HIS89 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00178 |
| Chain | Residue | Details |
| A | ASP88 | |
| B | ASP88 | |
| C | ASP88 | |
| D | ASP88 | |
| E | ASP88 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 25 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00178 |
| Chain | Residue | Details |
| A | TRP22 | |
| B | HIS124 | |
| C | TRP22 | |
| C | ALA56 | |
| C | PHE80 | |
| C | SER113 | |
| C | HIS124 | |
| D | TRP22 | |
| D | ALA56 | |
| D | PHE80 | |
| D | SER113 | |
| A | ALA56 | |
| D | HIS124 | |
| E | TRP22 | |
| E | ALA56 | |
| E | PHE80 | |
| E | SER113 | |
| E | HIS124 | |
| A | PHE80 | |
| A | SER113 | |
| A | HIS124 | |
| B | TRP22 | |
| B | ALA56 | |
| B | PHE80 | |
| B | SER113 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rvv |
| Chain | Residue | Details |
| A | ASP88 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rvv |
| Chain | Residue | Details |
| B | ASP88 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rvv |
| Chain | Residue | Details |
| C | ASP88 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rvv |
| Chain | Residue | Details |
| D | ASP88 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rvv |
| Chain | Residue | Details |
| E | ASP88 |
