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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | CYS90 |
| A | CYS93 |
| A | HIS115 |
| A | CYS118 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | CYS107 |
| A | CYS110 |
| A | CYS136 |
| A | CYS139 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 403 |
| Chain | Residue |
| A | CYS191 |
| A | HIS212 |
| A | CYS215 |
| A | CYS189 |
| 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 ZN B 401 |
| Chain | Residue |
| B | CYS189 |
| B | CYS191 |
| B | HIS212 |
| B | CYS215 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 402 |
| Chain | Residue |
| B | CYS204 |
| B | CYS207 |
| B | CYS234 |
| B | CYS237 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 403 |
| Chain | Residue |
| B | CYS90 |
| B | CYS93 |
| B | HIS115 |
| B | CYS118 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 404 |
| Chain | Residue |
| B | CYS107 |
| B | CYS110 |
| B | CYS136 |
| B | CYS139 |
Functional Information from PROSITE/UniProt
| site_id | PS01359 |
| Number of Residues | 50 |
| Details | ZF_PHD_1 Zinc finger PHD-type signature. CcvCrsetvvpgnrl..................................VsCek..Crha.YHqdChvprapapgegegas..............................WvCrqC |
| Chain | Residue | Details |
| A | CYS90-CYS139 | |
| A | CYS189-CYS237 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 57 |
| Details | Domain: {"description":"Tudor"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 55 |
| Details | Zinc finger: {"description":"PHD-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 108 |
| Details | Zinc finger: {"description":"PHD-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]} |
5XFQ
