2Z02
Crystal structure of phosphoribosylaminoimidazolesuccinocarboxamide synthase wit ATP from Methanocaldococcus jannaschii
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 | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 512 |
| Chain | Residue |
| A | ARG100 |
| A | SER106 |
| A | ARG109 |
| A | ARG206 |
| A | HOH1554 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 513 |
| Chain | Residue |
| A | HOH1596 |
| A | HOH1673 |
| A | HOH1676 |
| B | ASN139 |
| B | GLU140 |
| B | HOH2197 |
| A | ASN139 |
| A | GLU140 |
| A | HOH1530 |
| A | HOH1547 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 514 |
| Chain | Residue |
| B | ARG100 |
| B | GLY105 |
| B | SER106 |
| B | ARG206 |
| B | CIT2181 |
| B | HOH2204 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP A 1527 |
| Chain | Residue |
| A | TYR15 |
| A | GLY17 |
| A | LYS18 |
| A | ALA19 |
| A | LYS20 |
| A | ILE22 |
| A | HIS75 |
| A | LYS88 |
| A | VAL90 |
| A | ILE92 |
| A | LYS129 |
| A | GLU185 |
| A | ASP198 |
| A | HOH1595 |
| A | HOH1624 |
| A | HOH1669 |
| A | HOH1675 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ATP B 1526 |
| Chain | Residue |
| B | TYR15 |
| B | GLY17 |
| B | LYS18 |
| B | ALA19 |
| B | LYS20 |
| B | ILE22 |
| B | HIS75 |
| B | LYS88 |
| B | VAL90 |
| B | ILE92 |
| B | LYS129 |
| B | GLU185 |
| B | ASP198 |
| B | HOH2243 |
| B | HOH2270 |
| B | HOH2316 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CIT B 2181 |
| Chain | Residue |
| B | ILE98 |
| B | ASP181 |
| B | PHE182 |
| B | LYS183 |
| B | PRO202 |
| B | ASP203 |
| B | MET205 |
| B | ARG206 |
| B | ASP217 |
| B | LYS218 |
| B | ASP219 |
| B | ARG222 |
| B | SO4514 |
Functional Information from PROSITE/UniProt
