1R6X
The Crystal Structure of a Truncated Form of Yeast ATP Sulfurylase, Lacking the C-Terminal APS Kinase-like Domain, in complex with Sulfate
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2002 |
| Chain | Residue |
| A | GLN195 |
| A | ARG197 |
| A | ALA293 |
| A | HOH4071 |
| A | HOH4111 |
| A | HOH4205 |
| A | HOH4393 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2004 |
| Chain | Residue |
| A | ASP168 |
| A | ARG173 |
| A | HOH4184 |
| A | HOH4265 |
| A | HOH4407 |
| A | HIS166 |
| A | TYR167 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2005 |
| Chain | Residue |
| A | ARG205 |
| A | ARG213 |
| A | HOH4364 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 3000 |
| Chain | Residue |
| A | ASP168 |
| A | HIS235 |
| A | HIS236 |
| A | HOH4265 |
| A | HOH4355 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| 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_FI2 |
| Number of Residues | 10 |
| 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_FI3 |
| Number of Residues | 2 |
| 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_FI4 |
| Number of Residues | 1 |
| 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 | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| A | HIS204 | |
| A | HIS201 | |
| A | ARG197 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| A | ARG290 |
| 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 |
