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2Z6Q

Ternary structure of Arg165Ala M.HhaI C5-Cytosine DNA methyltransferase with unmodified DNA and AdoHcy

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
A0051719molecular_functionDNA (cytosine-5-)-methyltransferase activity, acting on CpN substrates
A0051720molecular_functionDNA (cytosine-5-)-methyltransferase activity, acting on CpNpG substrates
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE DCZ A 427
ChainResidue
ACYS81
AASN304
AHOH346
AHOH383
DDG426
EHOH347
EDG428
ASER85
AGLU119
AASN120
AVAL121
AARG163
AGLU164
AALA165
ATHR250

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAH A 328
ChainResidue
APHE18
AALA19
ALEU21
AGLY23
AASN39
AGLU40
ATRP41
AASP42
AASP60
AILE61
AGLY78
APRO80
ALEU100
AASN304
ASER305
AHOH338
AHOH345
AHOH377
AHOH385
DDT421

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
AALA165attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity

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PDB entries from 2024-11-06

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