4DNX
The structure of the ATP sulfurylase from Allochromatium vinosum in the open state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES A 401 |
| Chain | Residue |
| A | PRO12 |
| A | ARG13 |
| A | PHE14 |
| A | VAL15 |
| A | TYR16 |
| A | ASP17 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES B 401 |
| Chain | Residue |
| B | VAL15 |
| B | TYR16 |
| B | ASP17 |
| B | GLN162 |
| B | PRO12 |
| B | ARG13 |
| B | PHE14 |
