1SVU
Structure of the Q237W mutant of HhaI DNA methyltransferase: an insight into protein-protein interactions
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 600 |
| Chain | Residue |
| A | ARG13 |
| A | PRO70 |
| A | ASP71 |
| A | LYS114 |
| A | ARG172 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 601 |
| Chain | Residue |
| A | THR226 |
| A | ARG228 |
| A | TYR242 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SAH A 401 |
| Chain | Residue |
| A | ALA19 |
| A | GLY20 |
| A | LEU21 |
| A | GLY22 |
| A | GLY23 |
| A | ASN39 |
| A | GLU40 |
| A | TRP41 |
| A | ASP60 |
| A | ILE61 |
| A | THR62 |
| A | GLY78 |
| A | LEU100 |
| A | TYR285 |
| A | ASN304 |
| A | SER305 |
| A | PHE18 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAH B 402 |
| Chain | Residue |
| B | PHE18 |
| B | ALA19 |
| B | GLY20 |
| B | LEU21 |
| B | GLY23 |
| B | ASN39 |
| B | GLU40 |
| B | TRP41 |
| B | GLY59 |
| B | ASP60 |
| B | ILE61 |
| B | LEU100 |
| B | SER305 |
| B | VAL306 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 404 |
| Chain | Residue |
| B | LYS43 |
| B | GLU47 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 405 |
| Chain | Residue |
| B | VAL291 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX A 602 |
| Chain | Residue |
| A | ARG240 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX A 603 |
| Chain | Residue |
| A | TYR254 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 406 |
| Chain | Residue |
| B | ASP60 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 407 |
| Chain | Residue |
| A | LYS210 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX A 604 |
| Chain | Residue |
| A | LYS67 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX A 605 |
| Chain | Residue |
| A | ASN52 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 410 |
| Chain | Residue |
| B | GLU203 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 411 |
| Chain | Residue |
| B | PRO198 |
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 |
| A | 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 |
| A | LYS300-ILE318 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"7899082","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1mht |
| Chain | Residue | Details |
| A | GLU119 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mht |
| Chain | Residue | Details |
| B | CYS81 | |
| B | GLU119 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 293 |
| Chain | Residue | Details |
| 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 |
