2PAR
Crystal structure of the 5'-deoxynucleotidase YfbR mutant E72A complexed with Co(2+) and TMP
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 | HOH407 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO B 201 |
| Chain | Residue |
| B | HOH313 |
| B | HIS33 |
| B | HIS68 |
| B | ASP69 |
| B | ASP137 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TMP A 301 |
| Chain | Residue |
| A | ARG18 |
| A | TRP19 |
| A | HIS33 |
| A | ASP69 |
| A | ASP77 |
| A | LEU78 |
| A | THR80 |
| A | ASP137 |
| A | ALA141 |
| A | LEU163 |
| A | HOH407 |
| A | HOH414 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TMP B 301 |
| Chain | Residue |
| B | ARG18 |
| B | TRP19 |
| B | HIS33 |
| B | ASP69 |
| B | ASP77 |
| B | PRO79 |
| B | THR80 |
| B | PRO81 |
| B | ASP137 |
| B | ALA141 |
| B | HOH313 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 401 |
| Chain | Residue |
| A | GLU122 |
| A | TYR125 |
| A | LYS134 |
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 |
| B | ARG18 | |
| B | HIS33 | |
| B | ASP77 | |
| B | ASP137 | |
| A | ARG18 | |
| A | HIS33 | |
| A | ASP77 | |
| A | 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 |
