Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006974 | biological_process | cellular response to DNA damage stimulus |
A | 0031060 | biological_process | regulation of histone methylation |
A | 0035064 | molecular_function | methylated histone binding |
B | 0006974 | biological_process | cellular response to DNA damage stimulus |
B | 0031060 | biological_process | regulation of histone methylation |
B | 0035064 | molecular_function | methylated histone binding |
E | 0006974 | biological_process | cellular response to DNA damage stimulus |
E | 0031060 | biological_process | regulation of histone methylation |
E | 0035064 | molecular_function | methylated histone binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | CYS107 |
A | CYS110 |
A | CYS136 |
A | CYS139 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 402 |
Chain | Residue |
A | CYS189 |
A | CYS191 |
A | HIS212 |
A | CYS215 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN A 403 |
Chain | Residue |
A | CYS93 |
A | HIS115 |
A | CYS118 |
A | CYS90 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN A 404 |
Chain | Residue |
A | CYS204 |
A | CYS207 |
A | CYS234 |
A | CYS237 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue TRS A 405 |
Chain | Residue |
A | TRP41 |
A | PHE65 |
A | ASP67 |
A | SER69 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue ZN B 401 |
Chain | Residue |
B | CYS107 |
B | CYS110 |
B | CYS136 |
B | CYS139 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN B 402 |
Chain | Residue |
B | CYS90 |
B | CYS93 |
B | HIS115 |
B | CYS118 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue ZN B 403 |
Chain | Residue |
B | CYS189 |
B | CYS191 |
B | HIS212 |
B | CYS215 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue ZN B 404 |
Chain | Residue |
B | CYS204 |
B | CYS207 |
B | CYS234 |
B | CYS237 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue TRS B 405 |
Chain | Residue |
B | TYR47 |
B | ASP67 |
B | PHE71 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue ZN E 401 |
Chain | Residue |
E | CYS90 |
E | CYS93 |
E | HIS115 |
E | CYS118 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue ZN E 402 |
Chain | Residue |
E | CYS189 |
E | CYS191 |
E | HIS212 |
E | CYS215 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue ZN E 403 |
Chain | Residue |
E | CYS107 |
E | CYS110 |
E | CYS136 |
E | CYS139 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue ZN E 404 |
Chain | Residue |
E | CYS204 |
E | CYS207 |
E | CYS234 |
E | CYS237 |
Functional Information from PROSITE/UniProt
site_id | PS01359 |
Number of Residues | 50 |
Details | ZF_PHD_1 Zinc finger PHD-type signature. CcvCrsetvvpgnrl..................................VsCek..Crha.YHqdChvprapapgegegts..............................WvCrqC |
Chain | Residue | Details |
A | CYS90-CYS139 | |
A | CYS189-CYS237 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU87-ALA142 | |
B | GLU87-ALA142 | |
E | GLU87-ALA142 | |
Chain | Residue | Details |
A | GLN186-GLY240 | |
B | GLN186-GLY240 | |
E | GLN186-GLY240 | |