1QGX
X-RAY STRUCTURE OF YEAST HAL2P
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006790 | biological_process | sulfur compound metabolic process |
| A | 0008441 | molecular_function | 3'(2'),5'-bisphosphate nucleotidase activity |
| A | 0009086 | biological_process | obsolete methionine biosynthetic process |
| A | 0016078 | biological_process | tRNA decay |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042538 | biological_process | hyperosmotic salinity response |
| A | 0046854 | biological_process | phosphatidylinositol phosphate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | GLU72 |
| A | ASP142 |
| A | ILE144 |
| A | PO4404 |
| A | HOH410 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | GLU72 |
| A | PO4404 |
| A | HOH408 |
| A | HOH409 |
| A | HOH411 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PO4 A 404 |
| Chain | Residue |
| A | GLU72 |
| A | ASP142 |
| A | ILE144 |
| A | ASP145 |
| A | GLY146 |
| A | THR147 |
| A | MG401 |
| A | MG403 |
| A | AMP405 |
| A | SO4406 |
| A | HOH414 |
| A | HOH760 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 406 |
| Chain | Residue |
| A | SER43 |
| A | PRO44 |
| A | LYS148 |
| A | HIS241 |
| A | PO4404 |
| A | AMP405 |
| A | HOH409 |
| A | HOH414 |
| A | HOH758 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE AMP A 405 |
| Chain | Residue |
| A | ASP142 |
| A | GLY240 |
| A | HIS241 |
| A | ASP263 |
| A | SER264 |
| A | LYS267 |
| A | ARG281 |
| A | TYR288 |
| A | GLU290 |
| A | ASP294 |
| A | PO4404 |
| A | SO4406 |
| A | HOH412 |
| A | HOH413 |
| A | HOH417 |
| A | HOH418 |
| A | HOH420 |
| A | HOH716 |
| A | HOH760 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME A 407 |
| Chain | Residue |
| A | SER84 |
| A | MET313 |
| A | CYS349 |
| A | ASP350 |
| A | GLN353 |
| A | HOH426 |
| site_id | S1 |
| Number of Residues | 3 |
| Details | MAGNESIUM BINDING SITE |
| Chain | Residue |
| A | ASP142 |
| A | ILE144 |
| A | GLU72 |
| site_id | S3 |
| Number of Residues | 1 |
| Details | MAGNESIUM BINDING SITE |
| Chain | Residue |
| A | GLU72 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12126627","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10656801","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12126627","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QGX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12126627","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KA1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12126627","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KA1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10656801","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12126627","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2001","submissionDatabase":"PDB data bank","title":"Hal2p: Ion selectivity and implications on inhibition mechanism.","authors":["Patel S.","Albert A.","Blundell T.L."]}},{"source":"PDB","id":"1K9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KA0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QGX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 12126627 |
| Chain | Residue | Details |
| A | ASP294 | |
| A | ASP49 | |
| A | THR147 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 904 |
| Chain | Residue | Details |
| A | ASP49 | proton acceptor, proton donor |
| A | GLU72 | metal ligand |
| A | ASP142 | metal ligand |
| A | ILE144 | metal ligand |
| A | ASP145 | metal ligand |
| A | THR147 | proton acceptor, proton donor, proton relay |
| A | ASP294 | metal ligand |
