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2C7O

HhaI DNA methyltransferase complex with 13mer oligonucleotide containing 2-aminopurine adjacent to the target base (PCGC:GMGC) and SAH

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003886molecular_functionDNA (cytosine-5-)-methyltransferase activity
A0008168molecular_functionmethyltransferase activity
A0009307biological_processDNA restriction-modification system
A0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1329
ChainResidue
APRO198
AASP199
AHOH2152
AHOH2288
AHOH2289
AHOH2290

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1330
ChainResidue
AHOH2226
AHOH2291
AHOH2292
APRO286
AASP287
ASER288

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1331
ChainResidue
ALYS193
AARG245
ALYS290
AHOH2143
AHOH2225
AHOH2294

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1332
ChainResidue
ALYS114
AARG172
AHOH2295

site_idAC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE SAH A 1328
ChainResidue
APHE18
AALA19
ALEU21
AGLY23
AASN39
AGLU40
ATRP41
AASP42
AASP60
AILE61
AGLY78
APRO80
AASN304
ASER305
AVAL306
AHOH2062
AHOH2243
AHOH2282
AHOH2283
AHOH2284
AHOH2285
AHOH2286

Functional Information from PROSITE/UniProt
site_idPS00094
Number of Residues13
DetailsC5_MTASE_1 C-5 cytosine-specific DNA methylases active site. DiLcaGfPCqAFS
ChainResidueDetails
AASP73-SER85

site_idPS00095
Number of Residues19
DetailsC5_MTASE_2 C-5 cytosine-specific DNA methylases C-terminal signature. KqfGNSVvInVlqyIaynI
ChainResidueDetails
ALYS300-ILE318

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:7899082
ChainResidueDetails
ACYS81

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mht
ChainResidueDetails
ACYS81
AGLU119

site_idMCSA1
Number of Residues4
DetailsM-CSA 293
ChainResidueDetails
ACYS81covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor
AGLU119attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity
AARG163attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
AARG165attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity

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PDB entries from 2024-07-17

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