4FGR
X-Ray Structure of SAICAR Synthetase (PurC) from Streptococcus pneumoniae complexed with ADP and Mg2+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | GLU178 |
| A | ASP191 |
| A | ADP302 |
| A | HOH486 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP A 302 |
| Chain | Residue |
| A | HIS68 |
| A | LYS81 |
| A | VAL83 |
| A | ILE85 |
| A | LYS122 |
| A | GLU178 |
| A | ASP191 |
| A | MG301 |
| A | HOH421 |
| A | TYR7 |
| A | GLY9 |
| A | LYS10 |
| A | ALA11 |
| A | LYS12 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 303 |
| Chain | Residue |
| A | ARG103 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 304 |
| Chain | Residue |
| A | ARG93 |
| A | SER99 |
| A | ARG199 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 301 |
| Chain | Residue |
| B | ASP191 |
| B | ADP302 |
| B | HOH455 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP B 302 |
| Chain | Residue |
| B | TYR7 |
| B | GLY9 |
| B | LYS10 |
| B | ALA11 |
| B | LYS12 |
| B | ILE14 |
| B | LYS81 |
| B | VAL83 |
| B | ILE85 |
| B | LYS122 |
| B | GLU178 |
| B | ASP191 |
| B | MG301 |
| B | HOH455 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 303 |
| Chain | Residue |
| B | ARG93 |
| B | SER99 |
| B | ARG199 |
| B | HOH417 |
| B | HOH474 |
Functional Information from PROSITE/UniProt
