4XRU
Structure of Pnkp1/Rnl/Hen1 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003690 | molecular_function | double-stranded DNA binding |
A | 0005524 | molecular_function | ATP binding |
A | 0006281 | biological_process | DNA repair |
A | 0046403 | molecular_function | polynucleotide 3'-phosphatase activity |
A | 0046404 | molecular_function | ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0047846 | molecular_function | deoxynucleotide 3'-phosphatase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005524 | molecular_function | ATP binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0001510 | biological_process | RNA methylation |
C | 0005737 | cellular_component | cytoplasm |
C | 0008168 | molecular_function | methyltransferase activity |
C | 0008171 | molecular_function | O-methyltransferase activity |
C | 0008173 | molecular_function | RNA methyltransferase activity |
C | 0016070 | biological_process | RNA metabolic process |
C | 0016740 | molecular_function | transferase activity |
C | 0030422 | biological_process | siRNA processing |
C | 0031047 | biological_process | regulatory ncRNA-mediated gene silencing |
C | 0032259 | biological_process | methylation |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003690 | molecular_function | double-stranded DNA binding |
D | 0005524 | molecular_function | ATP binding |
D | 0006281 | biological_process | DNA repair |
D | 0046403 | molecular_function | polynucleotide 3'-phosphatase activity |
D | 0046404 | molecular_function | ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0047846 | molecular_function | deoxynucleotide 3'-phosphatase activity |
E | 0000166 | molecular_function | nucleotide binding |
E | 0005524 | molecular_function | ATP binding |
E | 0046872 | molecular_function | metal ion binding |
F | 0001510 | biological_process | RNA methylation |
F | 0005737 | cellular_component | cytoplasm |
F | 0008168 | molecular_function | methyltransferase activity |
F | 0008171 | molecular_function | O-methyltransferase activity |
F | 0008173 | molecular_function | RNA methyltransferase activity |
F | 0016070 | biological_process | RNA metabolic process |
F | 0016740 | molecular_function | transferase activity |
F | 0030422 | biological_process | siRNA processing |
F | 0031047 | biological_process | regulatory ncRNA-mediated gene silencing |
F | 0032259 | biological_process | methylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue MG A 401 |
Chain | Residue |
A | ASP183 |
A | ASP185 |
A | ASP288 |
A | HOH506 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue ATP A 402 |
Chain | Residue |
A | LYS24 |
A | SER25 |
A | THR26 |
A | THR87 |
A | ARG122 |
B | ASN370 |
B | GLU372 |
A | ALA19 |
A | PRO20 |
A | GLY21 |
A | SER22 |
A | GLY23 |
site_id | AC3 |
Number of Residues | 19 |
Details | binding site for residue ATP B 501 |
Chain | Residue |
B | THR25 |
B | ILE26 |
B | GLU59 |
B | LYS60 |
B | LYS61 |
B | TYR62 |
B | TYR66 |
B | ARG83 |
B | GLU120 |
B | PHE234 |
B | GLU294 |
B | LYS299 |
B | LYS313 |
B | ARG315 |
B | LYS344 |
B | LEU394 |
B | MG505 |
B | HOH608 |
B | HOH620 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue MES B 502 |
Chain | Residue |
B | SER32 |
B | VAL33 |
B | GLU34 |
B | GLU43 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue GOL B 503 |
Chain | Residue |
B | GLU39 |
B | ARG315 |
B | ASN317 |
B | HOH618 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue GOL B 504 |
Chain | Residue |
B | THR78 |
B | ILE88 |
B | ASN89 |
B | LEU91 |
B | GLN93 |
B | LEU97 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue MG B 505 |
Chain | Residue |
B | GLY64 |
B | GLU120 |
B | ATP501 |
B | HOH606 |
B | HOH608 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue PO4 B 506 |
Chain | Residue |
B | ASN250 |
B | ASP251 |
B | ARG301 |
B | THR302 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue SAH C 501 |
Chain | Residue |
C | ARG253 |
C | GLY271 |
C | ASP296 |
C | THR297 |
C | THR337 |
C | GLU338 |
C | HIS342 |
C | THR344 |
C | LEU351 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue MG C 502 |
Chain | Residue |
C | GLN64 |
C | TYR122 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue PO4 C 503 |
Chain | Residue |
C | ASN369 |
C | GLY417 |
C | GLY424 |
C | GLU425 |
C | THR426 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue MG D 401 |
Chain | Residue |
D | ASP183 |
D | ASP185 |
D | ASP288 |
D | HOH507 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue ATP D 402 |
Chain | Residue |
D | PRO20 |
D | GLY21 |
D | GLY23 |
D | LYS24 |
D | SER25 |
D | THR26 |
E | ASN370 |
E | GLU372 |
site_id | AD5 |
Number of Residues | 15 |
Details | binding site for residue ATP E 501 |
Chain | Residue |
E | MG502 |
E | HOH613 |
E | THR25 |
E | ILE26 |
E | LYS60 |
E | LYS61 |
E | TYR62 |
E | TYR66 |
E | ARG83 |
E | GLU120 |
E | PHE234 |
E | GLU294 |
E | LYS313 |
E | ARG315 |
E | LEU394 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue MG E 502 |
Chain | Residue |
E | TYR62 |
E | GLU120 |
E | GLU294 |
E | ATP501 |
E | HOH607 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue PO4 E 503 |
Chain | Residue |
E | ASP110 |
E | TYR241 |
E | ARG245 |
site_id | AD8 |
Number of Residues | 10 |
Details | binding site for residue SAH F 501 |
Chain | Residue |
F | HIS250 |
F | GLY271 |
F | GLY273 |
F | ASP296 |
F | THR297 |
F | THR337 |
F | VAL339 |
F | ASN343 |
F | THR344 |
F | LEU351 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue MG F 502 |
Chain | Residue |
F | GLN64 |
F | TYR122 |
F | TYR181 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue PO4 F 503 |
Chain | Residue |
F | TYR57 |
F | HIS176 |
F | TYR181 |
F | TYR184 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue PO4 F 504 |
Chain | Residue |
F | ASN369 |
F | PRO395 |
F | GLY424 |
F | GLU425 |
F | THR426 |