Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003677 | molecular_function | DNA binding |
A | 0006304 | biological_process | DNA modification |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0009007 | molecular_function | site-specific DNA-methyltransferase (adenine-specific) activity |
A | 0009307 | biological_process | DNA restriction-modification system |
A | 0032259 | biological_process | methylation |
D | 0003676 | molecular_function | nucleic acid binding |
D | 0003677 | molecular_function | DNA binding |
D | 0006304 | biological_process | DNA modification |
D | 0008168 | molecular_function | methyltransferase activity |
D | 0009007 | molecular_function | site-specific DNA-methyltransferase (adenine-specific) activity |
D | 0009307 | biological_process | DNA restriction-modification system |
D | 0032259 | biological_process | methylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NEA A 500 |
Chain | Residue |
A | ALA47 |
A | HOH503 |
A | HOH504 |
A | HOH565 |
A | HOH581 |
A | HOH667 |
A | HOH699 |
B | DA606 |
A | GLU71 |
A | ILE72 |
A | ASP73 |
A | ALA88 |
A | ASP89 |
A | PHE90 |
A | ASN105 |
A | PRO107 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NEA D 501 |
Chain | Residue |
D | VAL21 |
D | ALA47 |
D | GLU71 |
D | ILE72 |
D | ALA88 |
D | ASP89 |
D | PHE90 |
D | ASN105 |
D | PRO107 |
D | PHE146 |
D | HOH515 |
D | HOH622 |
D | HOH658 |
E | DA606 |
Functional Information from PROSITE/UniProt
site_id | PS00092 |
Number of Residues | 7 |
Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. ILGNPPY |
Chain | Residue | Details |
A | ILE102-TYR108 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | THR23 | |
D | PRO107 | |
A | GLU45 | |
A | GLU71 | |
A | ASP89 | |
A | PRO107 | |
D | THR23 | |
D | GLU45 | |
D | GLU71 | |
D | ASP89 | |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | SITE: Important for catalytic activity => ECO:0007744|PDB:2ADM |
Chain | Residue | Details |
A | ASN105 | |
A | TYR108 | |
D | ASN105 | |
D | TYR108 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Important for catalytic activity; via amide nitrogen => ECO:0007744|PDB:2ADM |
Chain | Residue | Details |
A | PRO106 | |
D | PRO106 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 2adm |
Chain | Residue | Details |
A | PRO106 | |
A | ASN105 | |
A | TYR108 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 2adm |
Chain | Residue | Details |
D | PRO106 | |
D | ASN105 | |
D | TYR108 | |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 46 |
Chain | Residue | Details |
A | ASN105 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | PRO106 | activator, electrostatic stabiliser, hydrogen bond acceptor |
A | TYR108 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | PHE196 | steric role |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 46 |
Chain | Residue | Details |
D | ASN105 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
D | PRO106 | activator, electrostatic stabiliser, hydrogen bond acceptor |
D | TYR108 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
D | PHE196 | steric role |