1YN9
Crystal structure of baculovirus RNA 5'-phosphatase complexed with phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004651 | molecular_function | polynucleotide 5'-phosphatase activity |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004651 | molecular_function | polynucleotide 5'-phosphatase activity |
| B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| B | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0016311 | biological_process | dephosphorylation |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004651 | molecular_function | polynucleotide 5'-phosphatase activity |
| C | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| C | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| C | 0006470 | biological_process | protein dephosphorylation |
| C | 0016311 | biological_process | dephosphorylation |
| C | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 601 |
| Chain | Residue |
| A | CYS119 |
| A | HOH740 |
| A | THR120 |
| A | HIS121 |
| A | ILE123 |
| A | ASN124 |
| A | ARG125 |
| A | ARG159 |
| A | HOH637 |
| A | HOH675 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 602 |
| Chain | Residue |
| A | THR62 |
| A | ASN63 |
| A | THR64 |
| A | TYR67 |
| A | THR120 |
| A | ARG125 |
| A | HOH617 |
| A | HOH658 |
| A | HOH668 |
| A | HOH681 |
| A | HOH733 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 603 |
| Chain | Residue |
| B | CYS119 |
| B | THR120 |
| B | HIS121 |
| B | ILE123 |
| B | ASN124 |
| B | ARG125 |
| B | HOH662 |
| B | HOH664 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 B 604 |
| Chain | Residue |
| B | THR62 |
| B | ASN63 |
| B | THR64 |
| B | TYR67 |
| B | THR120 |
| B | ARG125 |
| B | HOH677 |
| B | HOH684 |
| B | HOH713 |
| B | HOH720 |
| B | HOH744 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C 605 |
| Chain | Residue |
| C | CYS119 |
| C | THR120 |
| C | HIS121 |
| C | ILE123 |
| C | ASN124 |
| C | ARG125 |
| C | HOH629 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 C 606 |
| Chain | Residue |
| C | THR62 |
| C | ASN63 |
| C | THR64 |
| C | TYR67 |
| C | THR120 |
| C | ARG125 |
| C | HOH641 |
| C | HOH682 |
Functional Information from PROSITE/UniProt
| site_id | PS00383 |
| Number of Residues | 11 |
| Details | TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCthGinRTG |
| Chain | Residue | Details |
| A | VAL117-GLY127 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 288 |
| Details | Domain: {"description":"Tyrosine-protein phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Site: {"description":"Essential for RNA triphosphatase activity","evidences":[{"source":"PubMed","id":"15713658","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
