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 | 0050340 | molecular_function | thymidylate 5'-phosphatase activity |
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 | 0050340 | molecular_function | thymidylate 5'-phosphatase activity |
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 | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18353368, ECO:0007744|PDB:2PAU |
Chain | Residue | Details |
A | ARG18 | |
A | HIS33 | |
A | ASP77 | |
A | ASP137 | |
B | ARG18 | |
B | HIS33 | |
B | ASP77 | |
B | ASP137 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18353368, ECO:0007744|PDB:2PAR, ECO:0007744|PDB:2PAU |
Chain | Residue | Details |
A | HIS68 | |
B | HIS68 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18353368 |
Chain | Residue | Details |
A | ASP69 | |
B | ASP69 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Appears to be important in orienting the phosphate for catalysis |
Chain | Residue | Details |
A | ARG18 | |
B | ARG18 |