2PEY
Crystal structure of deletion mutant of APS-kinase domain of human PAPS-synthetase 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0004020 | molecular_function | adenylylsulfate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0004020 | molecular_function | adenylylsulfate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADX A 400 |
| Chain | Residue |
| A | ARG92 |
| A | GLY184 |
| A | PHE185 |
| A | THR186 |
| A | HOH414 |
| A | HOH419 |
| A | HOH444 |
| A | HOH459 |
| A | PHE101 |
| A | ARG106 |
| A | ASN109 |
| A | PHE131 |
| A | ILE132 |
| A | SER133 |
| A | PRO134 |
| A | LEU173 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE DAT A 300 |
| Chain | Residue |
| A | LEU60 |
| A | GLY62 |
| A | ALA63 |
| A | GLY64 |
| A | LYS65 |
| A | THR66 |
| A | THR67 |
| A | ARG168 |
| A | THR204 |
| A | CYS207 |
| A | ASP208 |
| A | VAL209 |
| A | HOH414 |
| A | HOH432 |
| A | HOH443 |
| A | HOH452 |
| B | HIS163 |
| B | GLN167 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE DAT B 227 |
| Chain | Residue |
| A | HIS163 |
| A | GLN167 |
| B | LEU60 |
| B | GLY62 |
| B | ALA63 |
| B | GLY64 |
| B | LYS65 |
| B | THR66 |
| B | THR67 |
| B | VAL68 |
| B | ARG168 |
| B | VAL170 |
| B | THR204 |
| B | CYS207 |
| B | ASP208 |
| B | VAL209 |
| B | HOH251 |
| B | HOH263 |
| B | HOH277 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15755455","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17276460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17540769","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1X6V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XJQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XNJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PEY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PEZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17276460","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2OFX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17276460","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17540769","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2OFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PEZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15755455","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17276460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17540769","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1X6V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XJQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XNJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OFW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PEY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PEZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17276460","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OFX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
