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2C7P

HhaI DNA methyltransferase complex with oligonucleotide containing 2- aminopurine opposite to the target base (GCGC:GMPC) 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 Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1329
ChainResidue
APRO286
AASP287
ASER288
AHOH2191

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1330
ChainResidue
ALEU196
ALEU197
APRO198
AARG281

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1331
ChainResidue
AARG245
ALYS290
ALYS193

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1332
ChainResidue
ALYS114
AARG172
AHOH2231

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1333
ChainResidue
AASP199
AHOH2189
AHOH2233
AHOH2234
AHOH2236
AHOH2237

site_idAC6
Number of Residues23
DetailsBINDING SITE FOR RESIDUE SAH A 1328
ChainResidue
APHE18
AALA19
AGLY20
ALEU21
AGLY23
AASN39
AGLU40
ATRP41
AASP60
AILE61
AGLY78
APRO80
ATYR285
AASN304
ASER305
AVAL306
AHOH2049
AHOH2202
AHOH2204
AHOH2227
AHOH2228
AHOH2229
AHOH2230

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EPE A 1334
ChainResidue
AGLU3
AILE4
ALYS5
AASP6
ATYR316
ALYS325
APRO326
ATYR327
AHOH2216

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT A 1335
ChainResidue
ALYS150
AVAL151
ALEU152
AASN153
AASP156
ATYR157
APRO185
AHOH2100
AHOH2111
AHOH2238

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_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 2024-05-29

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