6UCA
Crystal structure of human ZCCHC4 in complex with SAH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008988 | molecular_function | rRNA (adenine-N6-)-methyltransferase activity |
A | 0031167 | biological_process | rRNA methylation |
A | 0032259 | biological_process | methylation |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008988 | molecular_function | rRNA (adenine-N6-)-methyltransferase activity |
B | 0031167 | biological_process | rRNA methylation |
B | 0032259 | biological_process | methylation |
C | 0003676 | molecular_function | nucleic acid binding |
C | 0008168 | molecular_function | methyltransferase activity |
C | 0008270 | molecular_function | zinc ion binding |
C | 0008988 | molecular_function | rRNA (adenine-N6-)-methyltransferase activity |
C | 0031167 | biological_process | rRNA methylation |
C | 0032259 | biological_process | methylation |
D | 0003676 | molecular_function | nucleic acid binding |
D | 0008168 | molecular_function | methyltransferase activity |
D | 0008270 | molecular_function | zinc ion binding |
D | 0008988 | molecular_function | rRNA (adenine-N6-)-methyltransferase activity |
D | 0031167 | biological_process | rRNA methylation |
D | 0032259 | biological_process | methylation |
E | 0003676 | molecular_function | nucleic acid binding |
E | 0008168 | molecular_function | methyltransferase activity |
E | 0008270 | molecular_function | zinc ion binding |
E | 0008988 | molecular_function | rRNA (adenine-N6-)-methyltransferase activity |
E | 0031167 | biological_process | rRNA methylation |
E | 0032259 | biological_process | methylation |
F | 0003676 | molecular_function | nucleic acid binding |
F | 0008168 | molecular_function | methyltransferase activity |
F | 0008270 | molecular_function | zinc ion binding |
F | 0008988 | molecular_function | rRNA (adenine-N6-)-methyltransferase activity |
F | 0031167 | biological_process | rRNA methylation |
F | 0032259 | biological_process | methylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue SAH A 1001 |
Chain | Residue |
A | ALA66 |
A | PRO201 |
A | ARG202 |
A | ASP225 |
A | ILE226 |
A | TYR242 |
A | ASN243 |
A | MET244 |
A | PHE245 |
A | ASP276 |
A | PRO278 |
A | ASN170 |
A | ALA171 |
A | GLN172 |
A | TYR173 |
A | LEU174 |
A | PHE175 |
A | GLY199 |
A | THR200 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 1002 |
Chain | Residue |
A | CYS40 |
A | HIS42 |
A | CYS64 |
A | CYS73 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ZN A 1003 |
Chain | Residue |
A | CYS125 |
A | THR127 |
A | CYS128 |
A | HIS140 |
A | HIS143 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN A 1004 |
Chain | Residue |
A | CYS380 |
A | CYS383 |
A | HIS393 |
A | CYS400 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN A 1005 |
Chain | Residue |
A | CYS394 |
A | CYS397 |
A | HIS410 |
A | CYS417 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue ZN A 1006 |
Chain | Residue |
A | CYS411 |
A | CYS414 |
A | HIS424 |
A | CYS431 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN A 1007 |
Chain | Residue |
A | CYS425 |
A | CYS428 |
A | HIS436 |
A | CYS438 |
site_id | AC8 |
Number of Residues | 18 |
Details | binding site for residue SAH B 1001 |
Chain | Residue |
B | ALA66 |
B | THR169 |
B | ASN170 |
B | ALA171 |
B | GLN172 |
B | TYR173 |
B | LEU174 |
B | PHE175 |
B | GLY199 |
B | PRO201 |
B | ARG202 |
B | ASP225 |
B | ILE226 |
B | TYR242 |
B | ASN243 |
B | MET244 |
B | PHE245 |
B | ASP276 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue ZN B 1002 |
Chain | Residue |
B | CYS40 |
B | HIS42 |
B | CYS64 |
B | CYS73 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ZN B 1003 |
Chain | Residue |
B | CYS125 |
B | CYS128 |
B | HIS140 |
B | HIS143 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue ZN B 1004 |
Chain | Residue |
B | CYS380 |
B | CYS383 |
B | HIS393 |
B | CYS400 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue ZN B 1005 |
Chain | Residue |
B | CYS394 |
B | CYS397 |
B | HIS410 |
B | CYS417 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue ZN B 1006 |
Chain | Residue |
B | CYS411 |
B | CYS414 |
B | HIS424 |
B | CYS431 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue ZN B 1007 |
Chain | Residue |
B | CYS425 |
B | CYS428 |
B | HIS436 |
B | CYS438 |
site_id | AD6 |
Number of Residues | 18 |
Details | binding site for residue SAH C 1001 |
Chain | Residue |
C | ILE226 |
C | TYR242 |
C | ASN243 |
C | MET244 |
C | ASP276 |
C | ALA66 |
C | THR169 |
C | ASN170 |
C | ALA171 |
C | GLN172 |
C | TYR173 |
C | LEU174 |
C | PHE175 |
C | GLY199 |
C | THR200 |
C | PRO201 |
C | ARG202 |
C | ASP225 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue ZN C 1002 |
Chain | Residue |
C | CYS40 |
C | HIS42 |
C | CYS64 |
C | CYS73 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue ZN C 1003 |
Chain | Residue |
C | CYS125 |
C | CYS128 |
C | HIS140 |
C | HIS143 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue ZN C 1004 |
Chain | Residue |
C | CYS380 |
C | CYS383 |
C | HIS393 |
C | CYS400 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue ZN C 1005 |
Chain | Residue |
C | CYS394 |
C | CYS397 |
C | HIS410 |
C | CYS417 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue ZN C 1006 |
Chain | Residue |
C | CYS411 |
C | CYS414 |
C | HIS424 |
C | CYS431 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue ZN C 1007 |
Chain | Residue |
C | CYS425 |
C | CYS428 |
C | HIS436 |
C | CYS438 |
site_id | AE4 |
Number of Residues | 19 |
Details | binding site for residue SAH D 1001 |
Chain | Residue |
D | ALA66 |
D | ASN170 |
D | ALA171 |
D | GLN172 |
D | TYR173 |
D | LEU174 |
D | PHE175 |
D | GLY199 |
D | THR200 |
D | PRO201 |
D | ARG202 |
D | ASP225 |
D | ILE226 |
D | TYR242 |
D | ASN243 |
D | MET244 |
D | PHE245 |
D | ASP276 |
D | PRO278 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue ZN D 1002 |
Chain | Residue |
D | CYS40 |
D | HIS42 |
D | CYS64 |
D | CYS73 |
site_id | AE6 |
Number of Residues | 5 |
Details | binding site for residue ZN D 1003 |
Chain | Residue |
D | CYS125 |
D | THR127 |
D | CYS128 |
D | HIS140 |
D | HIS143 |
site_id | AE7 |
Number of Residues | 4 |
Details | binding site for residue ZN D 1004 |
Chain | Residue |
D | CYS380 |
D | CYS383 |
D | HIS393 |
D | CYS400 |
site_id | AE8 |
Number of Residues | 4 |
Details | binding site for residue ZN D 1005 |
Chain | Residue |
D | CYS394 |
D | CYS397 |
D | HIS410 |
D | CYS417 |
site_id | AE9 |
Number of Residues | 4 |
Details | binding site for residue ZN D 1006 |
Chain | Residue |
D | CYS411 |
D | CYS414 |
D | HIS424 |
D | CYS431 |
site_id | AF1 |
Number of Residues | 4 |
Details | binding site for residue ZN D 1007 |
Chain | Residue |
D | CYS425 |
D | CYS428 |
D | HIS436 |
D | CYS438 |
site_id | AF2 |
Number of Residues | 21 |
Details | binding site for residue SAH E 1001 |
Chain | Residue |
E | ALA66 |
E | THR169 |
E | ASN170 |
E | ALA171 |
E | GLN172 |
E | TYR173 |
E | LEU174 |
E | PHE175 |
E | GLY199 |
E | THR200 |
E | PRO201 |
E | ARG202 |
E | LEU203 |
E | ASP225 |
E | ILE226 |
E | TYR242 |
E | ASN243 |
E | MET244 |
E | PHE245 |
E | ASP276 |
E | PRO278 |
site_id | AF3 |
Number of Residues | 4 |
Details | binding site for residue ZN E 1002 |
Chain | Residue |
E | CYS40 |
E | HIS42 |
E | CYS64 |
E | CYS73 |
site_id | AF4 |
Number of Residues | 4 |
Details | binding site for residue ZN E 1003 |
Chain | Residue |
E | CYS125 |
E | CYS128 |
E | HIS140 |
E | HIS143 |
site_id | AF5 |
Number of Residues | 4 |
Details | binding site for residue ZN E 1004 |
Chain | Residue |
E | CYS380 |
E | CYS383 |
E | HIS393 |
E | CYS400 |
site_id | AF6 |
Number of Residues | 4 |
Details | binding site for residue ZN E 1005 |
Chain | Residue |
E | CYS394 |
E | CYS397 |
E | HIS410 |
E | CYS417 |
site_id | AF7 |
Number of Residues | 4 |
Details | binding site for residue ZN E 1006 |
Chain | Residue |
E | CYS411 |
E | CYS414 |
E | HIS424 |
E | CYS431 |
site_id | AF8 |
Number of Residues | 4 |
Details | binding site for residue ZN E 1007 |
Chain | Residue |
E | CYS425 |
E | CYS428 |
E | HIS436 |
E | CYS438 |
site_id | AF9 |
Number of Residues | 22 |
Details | binding site for residue SAH F 1001 |
Chain | Residue |
F | ALA66 |
F | THR169 |
F | ASN170 |
F | ALA171 |
F | GLN172 |
F | TYR173 |
F | LEU174 |
F | PHE175 |
F | GLY199 |
F | THR200 |
F | PRO201 |
F | ARG202 |
F | LEU203 |
F | ASP225 |
F | ILE226 |
F | ASP227 |
F | TYR242 |
F | ASN243 |
F | MET244 |
F | PHE245 |
F | ASP276 |
F | PRO278 |
site_id | AG1 |
Number of Residues | 4 |
Details | binding site for residue ZN F 1002 |
Chain | Residue |
F | CYS40 |
F | HIS42 |
F | CYS64 |
F | CYS73 |
site_id | AG2 |
Number of Residues | 4 |
Details | binding site for residue ZN F 1003 |
Chain | Residue |
F | CYS125 |
F | CYS128 |
F | HIS140 |
F | HIS143 |
site_id | AG3 |
Number of Residues | 4 |
Details | binding site for residue ZN F 1004 |
Chain | Residue |
F | CYS380 |
F | CYS383 |
F | HIS393 |
F | CYS400 |
site_id | AG4 |
Number of Residues | 4 |
Details | binding site for residue ZN F 1005 |
Chain | Residue |
F | CYS394 |
F | CYS397 |
F | HIS410 |
F | CYS417 |
site_id | AG5 |
Number of Residues | 4 |
Details | binding site for residue ZN F 1006 |
Chain | Residue |
F | CYS411 |
F | CYS414 |
F | HIS424 |
F | CYS431 |
site_id | AG6 |
Number of Residues | 4 |
Details | binding site for residue ZN F 1007 |
Chain | Residue |
F | CYS425 |
F | CYS428 |
F | HIS436 |
F | CYS438 |
Functional Information from PROSITE/UniProt
site_id | PS00092 |
Number of Residues | 7 |
Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. MVTDPPF |
Chain | Residue | Details |
A | MET273-PHE279 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 252 |
Details | ZN_FING: GRF-type => ECO:0000255|PROSITE-ProRule:PRU01343 |
Chain | Residue | Details |
A | CYS40-LYS82 | |
B | CYS40-LYS82 | |
C | CYS40-LYS82 | |
D | CYS40-LYS82 | |
E | CYS40-LYS82 | |
F | CYS40-LYS82 |
site_id | SWS_FT_FI2 |
Number of Residues | 102 |
Details | ZN_FING: CCHC-type |
Chain | Residue | Details |
A | HIS443-ASN460 | |
B | HIS443-ASN460 | |
C | HIS443-ASN460 | |
D | HIS443-ASN460 | |
E | HIS443-ASN460 | |
F | HIS443-ASN460 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01343, ECO:0000269|PubMed:31695039, ECO:0007744|PDB:6UCA |
Chain | Residue | Details |
A | CYS40 | |
C | HIS42 | |
C | CYS64 | |
C | CYS73 | |
D | CYS40 | |
D | HIS42 | |
D | CYS64 | |
D | CYS73 | |
E | CYS40 | |
E | HIS42 | |
E | CYS64 | |
A | HIS42 | |
E | CYS73 | |
F | CYS40 | |
F | HIS42 | |
F | CYS64 | |
F | CYS73 | |
A | CYS64 | |
A | CYS73 | |
B | CYS40 | |
B | HIS42 | |
B | CYS64 | |
B | CYS73 | |
C | CYS40 |
site_id | SWS_FT_FI4 |
Number of Residues | 150 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31695039, ECO:0007744|PDB:6UCA |
Chain | Residue | Details |
A | CYS125 | |
A | CYS380 | |
D | CYS438 | |
E | CYS125 | |
E | CYS128 | |
E | HIS140 | |
E | HIS143 | |
E | GLN172 | |
E | ARG202 | |
E | ASP225 | |
E | ASN243 | |
E | ASP276 | |
A | CYS383 | |
E | CYS380 | |
E | CYS383 | |
E | HIS393 | |
E | CYS394 | |
E | CYS397 | |
E | CYS400 | |
E | HIS410 | |
E | CYS411 | |
E | CYS414 | |
E | CYS417 | |
A | HIS393 | |
E | HIS424 | |
E | CYS425 | |
E | CYS428 | |
E | CYS431 | |
E | HIS436 | |
E | CYS438 | |
F | CYS125 | |
F | CYS128 | |
F | HIS140 | |
F | HIS143 | |
A | CYS394 | |
F | GLN172 | |
F | ARG202 | |
F | ASP225 | |
F | ASN243 | |
F | ASP276 | |
F | CYS380 | |
F | CYS383 | |
F | HIS393 | |
F | CYS394 | |
F | CYS397 | |
A | CYS397 | |
F | CYS400 | |
F | HIS410 | |
F | CYS411 | |
F | CYS414 | |
F | CYS417 | |
F | HIS424 | |
F | CYS425 | |
F | CYS428 | |
F | CYS431 | |
F | HIS436 | |
A | CYS400 | |
F | CYS438 | |
A | HIS410 | |
A | CYS411 | |
A | CYS414 | |
A | CYS417 | |
A | CYS128 | |
A | HIS424 | |
A | CYS425 | |
A | CYS428 | |
A | CYS431 | |
A | HIS436 | |
A | CYS438 | |
B | CYS125 | |
B | CYS128 | |
B | HIS140 | |
B | HIS143 | |
A | HIS140 | |
B | GLN172 | |
B | ARG202 | |
B | ASP225 | |
B | ASN243 | |
B | ASP276 | |
B | CYS380 | |
B | CYS383 | |
B | HIS393 | |
B | CYS394 | |
B | CYS397 | |
A | HIS143 | |
B | CYS400 | |
B | HIS410 | |
B | CYS411 | |
B | CYS414 | |
B | CYS417 | |
B | HIS424 | |
B | CYS425 | |
B | CYS428 | |
B | CYS431 | |
B | HIS436 | |
A | GLN172 | |
B | CYS438 | |
C | CYS125 | |
C | CYS128 | |
C | HIS140 | |
C | HIS143 | |
C | GLN172 | |
C | ARG202 | |
C | ASP225 | |
C | ASN243 | |
C | ASP276 | |
A | ARG202 | |
C | CYS380 | |
C | CYS383 | |
C | HIS393 | |
C | CYS394 | |
C | CYS397 | |
C | CYS400 | |
C | HIS410 | |
C | CYS411 | |
C | CYS414 | |
C | CYS417 | |
A | ASP225 | |
C | HIS424 | |
C | CYS425 | |
C | CYS428 | |
C | CYS431 | |
C | HIS436 | |
C | CYS438 | |
D | CYS125 | |
D | CYS128 | |
D | HIS140 | |
D | HIS143 | |
A | ASN243 | |
D | GLN172 | |
D | ARG202 | |
D | ASP225 | |
D | ASN243 | |
D | ASP276 | |
D | CYS380 | |
D | CYS383 | |
D | HIS393 | |
D | CYS394 | |
D | CYS397 | |
A | ASP276 | |
D | CYS400 | |
D | HIS410 | |
D | CYS411 | |
D | CYS414 | |
D | CYS417 | |
D | HIS424 | |
D | CYS425 | |
D | CYS428 | |
D | CYS431 | |
D | HIS436 |