Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008270 | molecular_function | zinc ion binding |
A | 0042054 | molecular_function | histone methyltransferase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0042054 | molecular_function | histone methyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 501 |
Chain | Residue |
A | CYS205 |
A | CYS208 |
A | CYS216 |
A | HIS219 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 502 |
Chain | Residue |
A | CYS390 |
A | CYS393 |
A | HIS406 |
A | HIS411 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 501 |
Chain | Residue |
B | CYS208 |
B | CYS216 |
B | HIS219 |
B | CYS205 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 502 |
Chain | Residue |
B | CYS390 |
B | CYS393 |
B | HIS406 |
B | HIS411 |
Functional Information from PROSITE/UniProt
site_id | PS00028 |
Number of Residues | 22 |
Details | ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cps..CclaFssqkflsqHvern.H |
Chain | Residue | Details |
A | CYS390-HIS411 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS388-HIS411 | |
B | HIS388-HIS411 | |
Chain | Residue | Details |
A | CYS205 | |
A | CYS208 | |
A | CYS216 | |
A | HIS219 | |
B | CYS205 | |
B | CYS208 | |
B | CYS216 | |
B | HIS219 | |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|Ref.10 |
Chain | Residue | Details |
A | ALA256 | |
A | TYR291 | |
A | ASN320 | |
B | ALA256 | |
B | TYR291 | |
B | ASN320 | |
Chain | Residue | Details |
A | ASN288 | |
A | TYR357 | |
B | ASN288 | |
B | TYR357 | |
Chain | Residue | Details |
A | CYS390 | |
A | CYS393 | |
A | HIS406 | |
A | HIS411 | |
B | CYS390 | |
B | CYS393 | |
B | HIS406 | |
B | HIS411 | |
Chain | Residue | Details |
A | LYS368 | |
B | LYS368 | |
Chain | Residue | Details |
A | LYS372 | |
A | LYS374 | |
B | LYS372 | |
B | LYS374 | |