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5LOD

Crystal structure of HhaI DNA methyltransferase in APO form

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
B0003677molecular_functionDNA binding
B0003886molecular_functionDNA (cytosine-5-)-methyltransferase activity
B0008168molecular_functionmethyltransferase activity
B0009307biological_processDNA restriction-modification system
B0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SO4 B 401
ChainResidue
BLEU155
BASP156
BPHE186
BLEU188
BPRO224
BHOH507
BHOH534

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 B 402
ChainResidue
BLYS193
BARG245

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 B 403
ChainResidue
BGLY238
BTHR250
BSER252
BLYS261
BHOH599

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 401
ChainResidue
ALEU155
AASP156
APHE186
ALEU188
APRO224
AHOH554

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 402
ChainResidue
AASN52
ASER288
ATYR289

Functional Information from PROSITE/UniProt
site_idPS00094
Number of Residues13
DetailsC5_MTASE_1 C-5 cytosine-specific DNA methylases active site. DiLcaGfPCqAFS
ChainResidueDetails
BASP73-SER85

site_idPS00095
Number of Residues19
DetailsC5_MTASE_2 C-5 cytosine-specific DNA methylases C-terminal signature. KqfGNSVvInVlqyIaynI
ChainResidueDetails
BLYS300-ILE318

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:7899082
ChainResidueDetails
BCYS81
ACYS81

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 293
ChainResidueDetails
BCYS81covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor
BGLU119attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity
BARG163attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
BARG165attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity

site_idMCSA2
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

222036

PDB entries from 2024-07-03

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