2PAU
Crystal structure of the 5'-deoxynucleotidase YfbR mutant E72A complexed with Co(2+) and dAMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0002953 | molecular_function | 5'-deoxynucleotidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006226 | biological_process | dUMP biosynthetic process |
| A | 0010139 | biological_process | pyrimidine deoxyribonucleotide salvage |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050897 | molecular_function | cobalt ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0002953 | molecular_function | 5'-deoxynucleotidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006226 | biological_process | dUMP biosynthetic process |
| B | 0010139 | biological_process | pyrimidine deoxyribonucleotide salvage |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050897 | molecular_function | cobalt ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 201 |
| Chain | Residue |
| A | HIS33 |
| A | HIS68 |
| A | ASP69 |
| A | ASP137 |
| A | HOH425 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 201 |
| Chain | Residue |
| B | HIS33 |
| B | HIS68 |
| B | ASP69 |
| B | ASP137 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE D5M A 301 |
| Chain | Residue |
| A | ARG18 |
| A | TRP19 |
| A | HIS33 |
| A | ASP69 |
| A | ASP77 |
| A | PRO79 |
| A | THR80 |
| A | ASP137 |
| A | HOH425 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE D5M B 301 |
| Chain | Residue |
| B | ARG18 |
| B | TRP19 |
| B | HIS33 |
| B | ASP69 |
| B | ASP77 |
| B | LEU78 |
| B | PRO79 |
| B | THR80 |
| B | PRO81 |
| B | ASP137 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 401 |
| Chain | Residue |
| A | GLU122 |
| A | TYR125 |
| A | LYS134 |
| A | ASP137 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18353368","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PAU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18353368","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PAU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18353368","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Appears to be important in orienting the phosphate for catalysis"} |
| Chain | Residue | Details |
