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 | 16 |
| Details | BINDING SITE FOR RESIDUE ADX A 401 |
| Chain | Residue |
| A | GLY137 |
| A | LYS218 |
| A | LEU220 |
| A | GLY231 |
| A | PHE232 |
| A | THR233 |
| A | ANP402 |
| A | HOH571 |
| A | ARG141 |
| A | PHE150 |
| A | ARG155 |
| A | ASN158 |
| A | LEU180 |
| A | ILE181 |
| A | SER182 |
| A | PRO183 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ANP A 402 |
| Chain | Residue |
| A | LEU109 |
| A | SER110 |
| A | GLY111 |
| A | SER112 |
| A | GLY113 |
| A | LYS114 |
| A | SER115 |
| A | THR116 |
| A | ILE181 |
| A | ARG215 |
| A | PRO217 |
| A | LYS218 |
| A | THR255 |
| A | PRO257 |
| A | MET260 |
| A | ADX401 |
| A | MG403 |
| A | HOH541 |
| A | HOH570 |
| A | HOH571 |
| A | HOH575 |
| A | HOH588 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | SER115 |
| A | ANP402 |
| A | HOH509 |
| A | HOH541 |
| A | HOH575 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADX B 301 |
| Chain | Residue |
| B | GLY137 |
| B | ARG141 |
| B | PHE150 |
| B | ARG155 |
| B | ASN158 |
| B | ILE159 |
| B | LEU180 |
| B | ILE181 |
| B | SER182 |
| B | PRO183 |
| B | LYS218 |
| B | LEU220 |
| B | PHE232 |
| B | ANP302 |
| B | HOH427 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ANP B 302 |
| Chain | Residue |
| B | LEU109 |
| B | SER110 |
| B | GLY111 |
| B | SER112 |
| B | GLY113 |
| B | LYS114 |
| B | SER115 |
| B | THR116 |
| B | ILE181 |
| B | ARG215 |
| B | PRO217 |
| B | LYS218 |
| B | THR255 |
| B | PRO257 |
| B | MET260 |
| B | ADX301 |
| B | MG303 |
| B | HOH427 |
| B | HOH439 |
| B | HOH443 |
| B | HOH497 |
| B | HOH536 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 303 |
| Chain | Residue |
| B | SER115 |
| B | ANP302 |
| B | HOH439 |
| B | HOH443 |
| B | HOH474 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADX C 301 |
| Chain | Residue |
| C | LYS230 |
| C | GLY231 |
| C | PHE232 |
| C | THR233 |
| C | ANP302 |
| C | HOH475 |
| 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 | LEU220 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ANP C 302 |
| Chain | Residue |
| C | LEU109 |
| C | SER110 |
| C | GLY111 |
| C | SER112 |
| C | GLY113 |
| C | LYS114 |
| C | SER115 |
| C | THR116 |
| C | ASP138 |
| C | ARG215 |
| C | PRO217 |
| C | LYS218 |
| C | THR255 |
| C | PRO257 |
| C | MET260 |
| C | ADX301 |
| C | MG303 |
| C | HOH446 |
| C | HOH457 |
| C | HOH465 |
| C | HOH471 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 303 |
| Chain | Residue |
| C | SER115 |
| C | ANP302 |
| C | HOH431 |
| C | HOH446 |
| C | HOH471 |
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 | |
