3NUA
Crystal Structure of Phosphoribosylaminoimidazole-Succinocarboxamide Synthase from Clostridium perfringens
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004639 | molecular_function | phosphoribosylaminoimidazolesuccinocarboxamide synthase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0009236 | biological_process | cobalamin biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| B | 0004639 | molecular_function | phosphoribosylaminoimidazolesuccinocarboxamide synthase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0009236 | biological_process | cobalamin biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP A 241 |
| Chain | Residue |
| A | TYR9 |
| A | ILE87 |
| A | LYS124 |
| A | GLU180 |
| A | ASP192 |
| A | GOL244 |
| A | HOH550 |
| A | HOH623 |
| A | HOH656 |
| A | HOH705 |
| A | HOH707 |
| A | GLY11 |
| A | HOH843 |
| A | LYS12 |
| A | ALA13 |
| A | LYS14 |
| A | ILE16 |
| A | HIS70 |
| A | LYS83 |
| A | VAL85 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE AMP A 242 |
| Chain | Residue |
| A | GLU91 |
| A | ARG95 |
| A | GLY100 |
| A | SER101 |
| A | ASP176 |
| A | LYS178 |
| A | ASP197 |
| A | THR198 |
| A | CYS199 |
| A | ARG200 |
| A | ARG216 |
| A | CIT243 |
| A | HOH530 |
| A | HOH542 |
| A | HOH599 |
| A | HOH663 |
| A | HOH664 |
| A | HOH743 |
| A | HOH853 |
| A | HOH855 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CIT A 243 |
| Chain | Residue |
| A | LYS12 |
| A | THR34 |
| A | ALA35 |
| A | PHE36 |
| A | LYS212 |
| A | ARG216 |
| A | AMP242 |
| A | HOH725 |
| A | HOH743 |
| A | HOH808 |
| A | HOH816 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 244 |
| Chain | Residue |
| A | TYR9 |
| A | ADP241 |
| A | HOH563 |
| A | HOH611 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP B 241 |
| Chain | Residue |
| B | TYR9 |
| B | GLY11 |
| B | LYS12 |
| B | ALA13 |
| B | LYS14 |
| B | ILE16 |
| B | HIS70 |
| B | LYS83 |
| B | VAL85 |
| B | ILE87 |
| B | LYS124 |
| B | GLU180 |
| B | ASP192 |
| B | HOH584 |
| B | HOH624 |
| B | HOH634 |
| B | HOH698 |
| B | HOH702 |
| B | HOH715 |
| B | HOH730 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP B 242 |
| Chain | Residue |
| B | GLU91 |
| B | ARG95 |
| B | GLY100 |
| B | SER101 |
| B | ASP176 |
| B | LYS178 |
| B | ASP197 |
| B | THR198 |
| B | CYS199 |
| B | ARG200 |
| B | ARG216 |
| B | CIT243 |
| B | HOH531 |
| B | HOH565 |
| B | HOH600 |
| B | HOH642 |
| B | HOH756 |
| B | HOH791 |
| B | HOH794 |
| B | HOH827 |
| B | HOH828 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CIT B 243 |
| Chain | Residue |
| B | PHE36 |
| B | LYS212 |
| B | ARG216 |
| B | ADP242 |
| B | HOH565 |
| B | HOH591 |
| B | HOH791 |
| B | LYS12 |
| B | THR34 |
| B | ALA35 |
Functional Information from PROSITE/UniProt
