Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000103 | biological_process | sulfate assimilation |
A | 0004020 | molecular_function | adenylylsulfate kinase activity |
A | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
A | 0005524 | molecular_function | ATP binding |
B | 0000103 | biological_process | sulfate assimilation |
B | 0004020 | molecular_function | adenylylsulfate kinase activity |
B | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
B | 0005524 | molecular_function | ATP binding |
C | 0000103 | biological_process | sulfate assimilation |
C | 0004020 | molecular_function | adenylylsulfate kinase activity |
C | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
C | 0005524 | molecular_function | ATP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PPS A 574 |
Chain | Residue |
A | ASP434 |
A | ILE517 |
A | LYS527 |
A | GLY528 |
A | PHE529 |
A | HOH612 |
A | ARG437 |
A | PHE446 |
A | ARG451 |
A | ASN454 |
A | ILE477 |
A | ALA478 |
A | PRO479 |
A | ARG515 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PPS B 575 |
Chain | Residue |
B | MET405 |
B | ASP434 |
B | ARG437 |
B | PHE446 |
B | ARG451 |
B | ASN454 |
B | PRO476 |
B | ILE477 |
B | ALA478 |
B | PRO479 |
B | ARG515 |
B | LYS527 |
B | GLY528 |
B | PHE529 |
B | THR530 |
B | HOH604 |
B | HOH669 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PPS C 576 |
Chain | Residue |
C | ASP434 |
C | ARG437 |
C | PHE446 |
C | ARG451 |
C | ASN454 |
C | ILE455 |
C | PRO476 |
C | ILE477 |
C | ALA478 |
C | PRO479 |
C | ARG515 |
C | LYS527 |
C | GLY528 |
C | PHE529 |
C | HOH699 |
C | HOH740 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | THR198 | |
A | ARG199 | |
A | ASN200 | |
B | THR198 | |
B | ARG199 | |
B | ASN200 | |
C | THR198 | |
C | ARG199 | |
C | ASN200 | |
Chain | Residue | Details |
A | GLN197 | |
B | VAL333 | |
C | GLN197 | |
C | ARG199 | |
C | GLY291 | |
C | ALA295 | |
C | VAL333 | |
A | ARG199 | |
A | GLY291 | |
A | ALA295 | |
A | VAL333 | |
B | GLN197 | |
B | ARG199 | |
B | GLY291 | |
B | ALA295 | |
Chain | Residue | Details |
A | ASP434 | |
C | ARG451 | |
C | ILE477 | |
C | ARG515 | |
A | ARG451 | |
A | ILE477 | |
A | ARG515 | |
B | ASP434 | |
B | ARG451 | |
B | ILE477 | |
B | ARG515 | |
C | ASP434 | |
Chain | Residue | Details |
A | HIS203 | |
B | HIS203 | |
C | HIS203 | |
Chain | Residue | Details |
A | HIS206 | |
B | HIS206 | |
C | HIS206 | |
Chain | Residue | Details |
A | PHE330 | |
B | PHE330 | |
C | PHE330 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1j70 |
Chain | Residue | Details |
A | ARG199 | |
A | HIS206 | |
A | HIS203 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1j70 |
Chain | Residue | Details |
B | ARG199 | |
B | HIS206 | |
B | HIS203 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1j70 |
Chain | Residue | Details |
C | ARG199 | |
C | HIS206 | |
C | HIS203 | |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j70 |
Chain | Residue | Details |
A | ARG292 | |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j70 |
Chain | Residue | Details |
B | ARG292 | |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j70 |
Chain | Residue | Details |
C | ARG292 | |