2GKS
Crystal Structure of the Bi-functional ATP Sulfurylase-APS Kinase from Aquifex aeolicus, a Chemolithotrophic Thermophile
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 |
| A | 0006790 | biological_process | sulfur compound metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019379 | biological_process | sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) |
| A | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| 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 |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019379 | biological_process | sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) |
| B | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP A 900 |
| Chain | Residue |
| A | CYS382 |
| A | HOH920 |
| A | ALA383 |
| A | GLY384 |
| A | LYS385 |
| A | SER386 |
| A | THR387 |
| A | ARG486 |
| A | THR522 |
| A | LEU525 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP A 902 |
| Chain | Residue |
| A | PHE169 |
| A | GLN170 |
| A | THR171 |
| A | ARG172 |
| A | ASN173 |
| A | MET239 |
| A | GLY265 |
| A | ARG266 |
| A | HIS268 |
| A | ALA269 |
| A | GLU305 |
| A | GLU306 |
| A | LEU307 |
| A | HOH989 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP B 906 |
| Chain | Residue |
| B | PHE169 |
| B | GLN170 |
| B | THR171 |
| B | ARG172 |
| B | ASN173 |
| B | HIS179 |
| B | LEU182 |
| B | GLY265 |
| B | ARG266 |
| B | HIS268 |
| B | ALA269 |
| B | GLU305 |
| B | GLU306 |
| B | LEU307 |
| B | HOH984 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP B 904 |
| Chain | Residue |
| B | LEU380 |
| B | CYS382 |
| B | ALA383 |
| B | GLY384 |
| B | LYS385 |
| B | SER386 |
| B | THR387 |
| B | ARG486 |
| B | LYS496 |
| B | THR522 |
| B | LEU525 |
| B | HOH970 |
| B | HOH974 |
| B | HOH1030 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Phosphoserine intermediate => ECO:0000250 |
| Chain | Residue | Details |
| A | SER453 | |
| B | SER453 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY379 | |
| B | GLY379 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| A | HIS179 | |
| A | ARG172 | |
| A | HIS176 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| B | HIS179 | |
| B | ARG172 | |
| B | HIS176 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| A | ARG266 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| B | ARG266 |
