1J70
CRYSTAL STRUCTURE OF YEAST ATP SULFURYLASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000096 | biological_process | sulfur amino acid metabolic process |
| 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 | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0016740 | molecular_function | transferase 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 | 0000096 | biological_process | sulfur amino acid metabolic 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0016740 | molecular_function | transferase 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 |
| C | 0000096 | biological_process | sulfur amino acid metabolic process |
| C | 0000103 | biological_process | sulfate assimilation |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0019379 | biological_process | sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) |
| C | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 C 2443 |
| Chain | Residue |
| C | GLN195 |
| C | THR196 |
| C | ARG197 |
| C | MET263 |
| C | HIS274 |
| C | HIS292 |
| C | ALA293 |
| C | HOH2516 |
| C | HOH2687 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2444 |
| Chain | Residue |
| B | GLN195 |
| B | THR196 |
| B | ARG197 |
| B | MET263 |
| B | HIS292 |
| B | ALA293 |
| B | HOH2509 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2445 |
| Chain | Residue |
| A | GLN195 |
| A | THR196 |
| A | ARG197 |
| A | HIS274 |
| A | HIS292 |
| A | ALA293 |
| A | HOH2472 |
| A | HOH2560 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA C 1759 |
| Chain | Residue |
| C | THR38 |
| C | PRO39 |
| C | ARG40 |
| C | TYR144 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA C 1763 |
| Chain | Residue |
| C | HIS433 |
| C | ASN434 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 1765 |
| Chain | Residue |
| A | PRO39 |
| A | ARG40 |
| A | TYR144 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 498 |
| Details | Region: {"description":"N-terminal","evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11157739","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 675 |
| Details | Region: {"description":"Catalytic","evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11157739","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 351 |
| Details | Region: {"description":"Required for oligomerization; adenylyl-sulfate kinase-like","evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14983089","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11157739","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11157739","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_03106","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11157739","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"},{"source":"PubMed","id":"11157739","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 11724564, 107174, 10506138, 11157739, 14983089, 9915785 |
| Chain | Residue | Details |
| A | HIS204 | |
| A | HIS201 | |
| A | ARG197 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 11724564, 107174, 10506138, 11157739, 14983089, 9915785 |
| Chain | Residue | Details |
| B | HIS204 | |
| B | HIS201 | |
| B | ARG197 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 11724564, 107174, 10506138, 11157739, 14983089, 9915785 |
| Chain | Residue | Details |
| C | HIS204 | |
| C | HIS201 | |
| C | ARG197 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 287 |
| Chain | Residue | Details |
| A | THR196 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | ARG197 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | HIS201 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS204 | electrostatic stabiliser |
| A | ARG290 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 287 |
| Chain | Residue | Details |
| B | THR196 | electrostatic stabiliser, hydrogen bond donor, steric role |
| B | ARG197 | electrostatic stabiliser, hydrogen bond donor, steric role |
| B | HIS201 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS204 | electrostatic stabiliser |
| B | ARG290 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 287 |
| Chain | Residue | Details |
| C | THR196 | electrostatic stabiliser, hydrogen bond donor, steric role |
| C | ARG197 | electrostatic stabiliser, hydrogen bond donor, steric role |
| C | HIS201 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | HIS204 | electrostatic stabiliser |
| C | ARG290 | electrostatic stabiliser |
