1I2D
CRYSTAL STRUCTURE OF ATP SULFURYLASE FROM PENICILLIUM CHRYSOGENUM
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 ADX A 574 |
| Chain | Residue |
| A | PHE196 |
| A | ALA295 |
| A | MET332 |
| A | VAL333 |
| A | HOH616 |
| A | HOH735 |
| A | GLN197 |
| A | THR198 |
| A | ARG199 |
| A | ASN200 |
| A | HIS206 |
| A | GLY291 |
| A | ARG292 |
| A | HIS294 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADX A 575 |
| Chain | Residue |
| A | MET405 |
| A | ASP434 |
| A | ARG437 |
| A | PHE446 |
| A | ARG451 |
| A | ASN454 |
| A | PRO476 |
| A | ILE477 |
| A | ALA478 |
| A | PRO479 |
| A | LYS527 |
| A | GLY528 |
| A | PHE529 |
| A | THR530 |
| A | HOH634 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADX B 576 |
| Chain | Residue |
| B | PHE196 |
| B | GLN197 |
| B | THR198 |
| B | ARG199 |
| B | ASN200 |
| B | HIS206 |
| B | LEU209 |
| B | GLY291 |
| B | ARG292 |
| B | HIS294 |
| B | ALA295 |
| B | MET332 |
| B | VAL333 |
| B | HOH592 |
| B | HOH641 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADX B 577 |
| Chain | Residue |
| B | MET405 |
| B | ASP434 |
| B | ARG437 |
| B | PHE446 |
| B | ARG451 |
| B | ASN454 |
| B | PRO476 |
| B | ILE477 |
| B | ALA478 |
| B | PRO479 |
| B | ILE517 |
| B | LYS527 |
| B | GLY528 |
| B | PHE529 |
| B | THR530 |
| B | HOH578 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADX C 578 |
| Chain | Residue |
| C | PHE196 |
| C | GLN197 |
| C | THR198 |
| C | ARG199 |
| C | ASN200 |
| C | HIS206 |
| C | GLY291 |
| C | ARG292 |
| C | HIS294 |
| C | ALA295 |
| C | GLN331 |
| C | MET332 |
| C | VAL333 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADX C 579 |
| Chain | Residue |
| C | MET405 |
| C | GLY433 |
| C | ASP434 |
| C | ARG437 |
| C | PHE446 |
| C | ARG451 |
| C | ASN454 |
| C | PRO476 |
| C | ILE477 |
| C | ALA478 |
| C | PRO479 |
| C | LYS527 |
| C | GLY528 |
| C | PHE529 |
| C | THR530 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 534 |
| Details | Region: {"description":"Allosteric regulation domain; adenylyl-sulfate kinase-like","evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389593","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389593","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12426581","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389593","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Site: {"description":"Induces change in substrate recognition on ATP binding","evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
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 |
