4JA0
Crystal structure of the invertebrate bi-functional purine biosynthesis enzyme PAICS at 2.8 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
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 | 0016831 | molecular_function | carboxy-lyase activity |
A | 0016874 | molecular_function | ligase activity |
A | 0043727 | molecular_function | 5-amino-4-imidazole carboxylate lyase activity |
B | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
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 | 0016831 | molecular_function | carboxy-lyase activity |
B | 0016874 | molecular_function | ligase activity |
B | 0043727 | molecular_function | 5-amino-4-imidazole carboxylate lyase activity |
C | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
C | 0004639 | molecular_function | phosphoribosylaminoimidazolesuccinocarboxamide synthase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005829 | cellular_component | cytosol |
C | 0006164 | biological_process | purine nucleotide biosynthetic process |
C | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
C | 0016831 | molecular_function | carboxy-lyase activity |
C | 0016874 | molecular_function | ligase activity |
C | 0043727 | molecular_function | 5-amino-4-imidazole carboxylate lyase activity |
D | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
D | 0004639 | molecular_function | phosphoribosylaminoimidazolesuccinocarboxamide synthase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005829 | cellular_component | cytosol |
D | 0006164 | biological_process | purine nucleotide biosynthetic process |
D | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
D | 0016831 | molecular_function | carboxy-lyase activity |
D | 0016874 | molecular_function | ligase activity |
D | 0043727 | molecular_function | 5-amino-4-imidazole carboxylate lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | PRO31 |
A | GLY32 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 502 |
Chain | Residue |
A | SER144 |
A | GLU145 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 503 |
Chain | Residue |
A | ARG332 |
D | TYR379 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 504 |
Chain | Residue |
A | TYR167 |
A | ILE205 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 505 |
Chain | Residue |
A | LYS20 |
A | THR21 |
A | LYS22 |
A | GLY19 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 506 |
Chain | Residue |
A | ARG104 |
A | GLY109 |
A | SER110 |
A | PHE111 |
A | ARG217 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 501 |
Chain | Residue |
A | LYS152 |
B | PRO31 |
B | LYS93 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 502 |
Chain | Residue |
B | ARG332 |
B | LYS357 |
B | HOH614 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 503 |
Chain | Residue |
B | GLY19 |
B | LYS20 |
B | THR21 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 504 |
Chain | Residue |
B | ARG104 |
B | GLY109 |
B | SER110 |
B | ARG217 |
B | HOH609 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 501 |
Chain | Residue |
C | PRO31 |
C | GLY32 |
C | LYS93 |
D | LYS152 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 502 |
Chain | Residue |
B | TYR379 |
C | ARG332 |
C | HOH611 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 C 503 |
Chain | Residue |
C | LYS20 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 504 |
Chain | Residue |
C | ARG104 |
C | GLY109 |
C | SER110 |
C | ARG217 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 501 |
Chain | Residue |
D | PRO31 |
D | GLY32 |
D | LYS93 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 D 502 |
Chain | Residue |
D | ARG332 |
D | LYS357 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 503 |
Chain | Residue |
D | ARG104 |
D | THR108 |
D | GLY109 |
D | SER110 |
D | ARG217 |
Functional Information from PROSITE/UniProt