4ZCF
Structural basis of asymmetric DNA methylation and ATP-triggered long-range diffusion by EcoP15I
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008170 | molecular_function | N-methyltransferase activity |
| A | 0009007 | molecular_function | site-specific DNA-methyltransferase (adenine-specific) activity |
| A | 0009307 | biological_process | DNA restriction-modification system |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008170 | molecular_function | N-methyltransferase activity |
| B | 0009007 | molecular_function | site-specific DNA-methyltransferase (adenine-specific) activity |
| B | 0009307 | biological_process | DNA restriction-modification system |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0004386 | molecular_function | helicase activity |
| C | 0004518 | molecular_function | nuclease activity |
| C | 0004519 | molecular_function | endonuclease activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0009307 | biological_process | DNA restriction-modification system |
| C | 0015668 | molecular_function | type III site-specific deoxyribonuclease activity |
| C | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | binding site for residue MN A 701 |
| Chain | Residue |
| A | HIS201 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue MN A 702 |
| Chain | Residue |
| A | GLU213 |
| C | HIS168 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue AMP C 1001 |
| Chain | Residue |
| C | GLY122 |
| C | THR123 |
| C | PHE126 |
| C | ASP226 |
| C | GLU227 |
| C | ASP509 |
| C | ARG537 |
| C | GLN14 |
| C | GLY89 |
| C | LYS90 |
| C | THR91 |
| C | TYR92 |
| C | ILE119 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CA D 101 |
| Chain | Residue |
| B | HOH717 |
| B | HOH723 |
| D | DA8 |
| D | HOH202 |
Functional Information from PROSITE/UniProt
| site_id | PS00092 |
| Number of Residues | 7 |
| Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. IYIDPPY |
| Chain | Residue | Details |
| A | ILE120-TYR126 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Region: {"description":"Binding of S-adenosyl methionine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26067164","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZCF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
