2YWV
Crystal structure of SAICAR synthetase from Geobacillus kaustophilus
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 | 0005829 | cellular_component | cytosol |
| 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 | 0005829 | cellular_component | cytosol |
| 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 | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 541 |
| Chain | Residue |
| B | ARG95 |
| B | GLY100 |
| B | SER101 |
| B | ARG201 |
| B | HOH823 |
| B | HOH901 |
| B | HOH914 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 542 |
| Chain | Residue |
| B | ASN37 |
| B | LYS213 |
| B | ARG217 |
| B | HOH881 |
| B | HOH912 |
| B | ALA35 |
| B | PHE36 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 543 |
| Chain | Residue |
| A | ARG95 |
| A | GLY100 |
| A | SER101 |
| A | ARG201 |
| A | HOH807 |
| A | HOH821 |
| A | HOH904 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 544 |
| Chain | Residue |
| A | ALA35 |
| A | PHE36 |
| A | ASN37 |
| A | LYS213 |
| A | ARG217 |
| A | HOH858 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 545 |
| Chain | Residue |
| A | VAL97 |
| A | ARG164 |
| A | ARG173 |
| A | HOH793 |
| A | HOH826 |
| A | HOH957 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 546 |
| Chain | Residue |
| B | VAL97 |
| B | ARG173 |
| B | HOH779 |
| B | HOH799 |
| B | HOH820 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 548 |
| Chain | Residue |
| A | ARG105 |
| A | PRO131 |
| A | LEU132 |
| B | ARG105 |
| B | HOH782 |
| B | HOH933 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 701 |
| Chain | Residue |
| A | ASP193 |
| A | ADP600 |
| A | HOH706 |
| A | HOH709 |
| A | HOH787 |
| A | HOH798 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 702 |
| Chain | Residue |
| B | ADP601 |
| B | HOH708 |
| B | HOH709 |
| B | HOH713 |
| B | HOH812 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP A 600 |
| Chain | Residue |
| A | TYR9 |
| A | GLY11 |
| A | LYS12 |
| A | ALA13 |
| A | LYS14 |
| A | ILE16 |
| A | LEU25 |
| A | HIS70 |
| A | ARG83 |
| A | VAL85 |
| A | ILE87 |
| A | LYS124 |
| A | GLU180 |
| A | ASP193 |
| A | MG701 |
| A | HOH706 |
| A | HOH833 |
| A | HOH862 |
| site_id | BC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP B 601 |
| Chain | Residue |
| B | TYR9 |
| B | GLY11 |
| B | LYS12 |
| B | ALA13 |
| B | LYS14 |
| B | ILE16 |
| B | LEU25 |
| B | HIS70 |
| B | ARG83 |
| B | VAL85 |
| B | ILE87 |
| B | LYS124 |
| B | GLU180 |
| B | ASP193 |
| B | MG702 |
| B | HOH708 |
| B | HOH735 |
| B | HOH877 |
Functional Information from PROSITE/UniProt
