Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0004020 | molecular_function | adenylylsulfate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0004020 | molecular_function | adenylylsulfate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| C | 0000103 | biological_process | sulfate assimilation |
| C | 0004020 | molecular_function | adenylylsulfate kinase activity |
| C | 0005524 | molecular_function | ATP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADX A 301 |
| Chain | Residue |
| A | GLY137 |
| A | SER182 |
| A | PRO183 |
| A | LYS218 |
| A | ILE229 |
| A | GLY231 |
| A | PHE232 |
| A | THR233 |
| A | HOH406 |
| A | HOH534 |
| A | HOH549 |
| A | ASP138 |
| A | ARG141 |
| A | PHE150 |
| A | ARG155 |
| A | ASN158 |
| A | ILE159 |
| A | LEU180 |
| A | ILE181 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | LEU109 |
| A | SER110 |
| A | GLY111 |
| A | SER112 |
| A | GLY113 |
| A | LYS114 |
| A | SER115 |
| A | HOH424 |
| A | HOH452 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADX B 301 |
| Chain | Residue |
| B | GLY137 |
| B | ASP138 |
| B | ARG141 |
| B | PHE150 |
| B | ARG155 |
| B | ASN158 |
| B | LEU180 |
| B | ILE181 |
| B | SER182 |
| B | PRO183 |
| B | LYS218 |
| B | LEU220 |
| B | LYS230 |
| B | GLY231 |
| B | PHE232 |
| B | THR233 |
| B | HOH439 |
| B | HOH452 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 302 |
| Chain | Residue |
| B | LEU109 |
| B | GLY111 |
| B | SER112 |
| B | GLY113 |
| B | LYS114 |
| B | SER115 |
| B | HOH411 |
| B | HOH484 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADX C 301 |
| Chain | Residue |
| B | THR79 |
| B | ASN80 |
| B | ILE81 |
| C | GLY137 |
| C | ASP138 |
| C | ARG141 |
| C | PHE150 |
| C | ARG155 |
| C | ASN158 |
| C | LEU180 |
| C | ILE181 |
| C | SER182 |
| C | PRO183 |
| C | LYS218 |
| C | LYS230 |
| C | GLY231 |
| C | PHE232 |
| C | THR233 |
| C | HOH405 |
| C | HOH419 |
| C | HOH425 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 302 |
| Chain | Residue |
| C | LEU109 |
| C | GLY111 |
| C | SER112 |
| C | GLY113 |
| C | LYS114 |
| C | SER115 |
| C | HOH450 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Phosphoserine intermediate => ECO:0000250 |
| Chain | Residue | Details |
| A | SER182 | |
| B | SER182 | |
| C | SER182 | |
| Chain | Residue | Details |
| A | GLY108 | |
| B | GLY108 | |
| C | GLY108 | |
| Chain | Residue | Details |
| A | ASP138 | |
| B | GLY231 | |
| C | ASP138 | |
| C | ARG141 | |
| C | ARG155 | |
| C | ASN158 | |
| C | GLY231 | |
| A | ARG141 | |
| A | ARG155 | |
| A | ASN158 | |
| A | GLY231 | |
| B | ASP138 | |
| B | ARG141 | |
| B | ARG155 | |
| B | ASN158 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ILE181 | |
| B | ILE181 | |
| C | ILE181 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | SITE: Participates in a stacking interaction with the adenine ring of adenylyl-sulfate |
| Chain | Residue | Details |
| A | PHE150 | |
| B | PHE150 | |
| C | PHE150 | |
