5LOD
Crystal structure of HhaI DNA methyltransferase in APO form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003886 | molecular_function | DNA (cytosine-5-)-methyltransferase activity |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0009307 | biological_process | DNA restriction-modification system |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003886 | molecular_function | DNA (cytosine-5-)-methyltransferase activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0009307 | biological_process | DNA restriction-modification system |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| B | LEU155 |
| B | ASP156 |
| B | PHE186 |
| B | LEU188 |
| B | PRO224 |
| B | HOH507 |
| B | HOH534 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | LYS193 |
| B | ARG245 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| B | GLY238 |
| B | THR250 |
| B | SER252 |
| B | LYS261 |
| B | HOH599 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | LEU155 |
| A | ASP156 |
| A | PHE186 |
| A | LEU188 |
| A | PRO224 |
| A | HOH554 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | ASN52 |
| A | SER288 |
| A | TYR289 |
Functional Information from PROSITE/UniProt
| site_id | PS00094 |
| Number of Residues | 13 |
| Details | C5_MTASE_1 C-5 cytosine-specific DNA methylases active site. DiLcaGfPCqAFS |
| Chain | Residue | Details |
| B | ASP73-SER85 |
| site_id | PS00095 |
| Number of Residues | 19 |
| Details | C5_MTASE_2 C-5 cytosine-specific DNA methylases C-terminal signature. KqfGNSVvInVlqyIaynI |
| Chain | Residue | Details |
| B | LYS300-ILE318 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"7899082","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 293 |
| Chain | Residue | Details |
| A | CYS81 | covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| A | GLU119 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity |
| A | ARG163 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| A | ARG165 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 293 |
| Chain | Residue | Details |
| B | CYS81 | covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
| B | GLU119 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity |
| B | ARG163 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| B | ARG165 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
