Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 1101 |
| Chain | Residue |
| A | CYS829 |
| A | CYS832 |
| A | HIS849 |
| A | CYS852 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 1102 |
| Chain | Residue |
| A | CYS841 |
| A | CYS844 |
| A | CYS867 |
| A | CYS870 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue 7FU A 1103 |
| Chain | Residue |
| A | PHE924 |
| A | VAL928 |
| A | VAL932 |
| A | TYR935 |
| A | ILE972 |
| A | ASN975 |
| A | CYS976 |
| A | ASN980 |
| A | HOH1219 |
| A | HOH1249 |
| A | ALA923 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 1104 |
| Chain | Residue |
| A | PRO861 |
| A | SER862 |
| A | GLY863 |
| A | GLU981 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 1101 |
| Chain | Residue |
| B | CYS829 |
| B | CYS832 |
| B | HIS849 |
| B | CYS852 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 1102 |
| Chain | Residue |
| B | CYS841 |
| B | CYS844 |
| B | CYS867 |
| B | CYS870 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue 7FU B 1103 |
| Chain | Residue |
| B | ALA923 |
| B | PHE924 |
| B | VAL928 |
| B | VAL932 |
| B | TYR935 |
| B | ILE972 |
| B | ASN975 |
| B | CYS976 |
| B | ASN980 |
| B | HOH1213 |
| B | HOH1230 |
| B | HOH1234 |
| B | HOH1237 |
Functional Information from PROSITE/UniProt
| site_id | PS00633 |
| Number of Residues | 62 |
| Details | BROMODOMAIN_1 Bromodomain signature. HemSlafqDpvpltvpDYYkiIknpMdlstIkkrlqedysmYskpedfvadfrl.IfqNCaeF |
| Chain | Residue | Details |
| A | HIS918-PHE979 | |
| site_id | PS01359 |
| Number of Residues | 42 |
| Details | ZF_PHD_1 Zinc finger PHD-type signature. CavCqnggel.......................................LcCek..Cpkv.FHlsChvptltnfpsge.................................WiCtfC |
| Chain | Residue | Details |
| A | CYS829-CYS870 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 94 |
| Details | Zinc finger: {"description":"PHD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Region: {"description":"Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Region: {"description":"Interaction with histone H3 that is acetylated at 'Lys-23' (H3K23ac)"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"}]} |