Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MPD B 101 |
Chain | Residue |
B | 1CC5 |
B | HOH276 |
C | HIS158 |
C | ALA161 |
C | HOH350 |
E | MPD101 |
F | ALA161 |
F | HIS162 |
F | GLY164 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ACT B 102 |
Chain | Residue |
A | HOH139 |
A | HOH158 |
B | DA10 |
B | DT11 |
B | HOH241 |
B | HOH243 |
B | HOH264 |
B | HOH265 |
B | HOH272 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA B 103 |
Chain | Residue |
A | HOH159 |
A | HOH160 |
A | HOH161 |
B | HOH268 |
B | HOH269 |
B | HOH270 |
B | HOH271 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 201 |
Chain | Residue |
C | CYS170 |
C | CYS173 |
C | HIS186 |
C | HIS190 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 202 |
Chain | Residue |
C | CYS142 |
C | PHE144 |
C | CYS145 |
C | HIS158 |
C | HIS162 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD C 203 |
Chain | Residue |
C | PHE141 |
C | ASN184 |
C | HOH344 |
C | HOH347 |
C | HOH358 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT C 204 |
Chain | Residue |
A | HOH109 |
C | LEU163 |
C | TYR165 |
C | HOH390 |
F | HIS190 |
F | HOH372 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT C 205 |
Chain | Residue |
C | HIS190 |
C | HOH388 |
D | HOH143 |
F | TYR165 |
F | HOH393 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MPD E 101 |
Chain | Residue |
B | MPD101 |
C | ALA161 |
C | HIS162 |
C | GLY164 |
C | HOH385 |
C | HOH393 |
E | 1CC5 |
F | HIS158 |
F | ALA161 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT E 102 |
Chain | Residue |
D | HOH132 |
E | DA10 |
E | DT11 |
E | HOH256 |
E | HOH277 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA E 103 |
Chain | Residue |
D | HOH145 |
D | HOH146 |
D | HOH147 |
E | HOH206 |
E | HOH279 |
E | HOH280 |
E | HOH281 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 201 |
Chain | Residue |
F | CYS170 |
F | CYS173 |
F | HIS186 |
F | HIS190 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 202 |
Chain | Residue |
F | CYS142 |
F | PHE144 |
F | CYS145 |
F | HIS158 |
F | HIS162 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD F 203 |
Chain | Residue |
D | HOH133 |
F | PHE141 |
F | ASN184 |
F | HOH345 |
F | HOH360 |
F | HOH374 |
Functional Information from PROSITE/UniProt
site_id | PS00028 |
Number of Residues | 21 |
Details | ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cnf..CgktYrdasglsrHrra..H |
Chain | Residue | Details |
C | CYS142-HIS162 | |
C | CYS170-HIS190 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
C | PHE140-HIS162 | |
F | PHE140-HIS162 | |
Chain | Residue | Details |
C | ARG168-HIS190 | |
F | ARG168-HIS190 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Crucial for 5-methylcytosine recognition |
Chain | Residue | Details |
C | ARG178 | |
F | ARG178 | |