5MHT

TERNARY STRUCTURE OF HHAI METHYLTRANSFERASE WITH HEMIMETHYLATED DNA AND ADOHCY

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003886	molecular_function	DNA (cytosine-5-)-methyltransferase activity
A	0008168	molecular_function	methyltransferase activity
A	0009307	biological_process	DNA restriction-modification system
A	0032259	biological_process	methylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE SAH A 328

Chain	Residue
A	PHE18
A	ILE61
A	GLY78
A	ASN304
A	SER305
A	HOH332
A	HOH333
A	HOH338
A	HOH340
A	HOH367
A	HOH384
A	ALA19
A	GLY20
A	LEU21
A	GLY23
A	ASN39
A	GLU40
A	TRP41
A	ASP60

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Functional Information from PROSITE/UniProt

site_id	PS00094
Number of Residues	13
Details	C5_MTASE_1 C-5 cytosine-specific DNA methylases active site. DiLcaGfPCqAFS

Chain	Residue	Details
A	ASP73-SER85

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site_id	PS00095
Number of Residues	19
Details	C5_MTASE_2 C-5 cytosine-specific DNA methylases C-terminal signature. KqfGNSVvInVlqyIaynI

Chain	Residue	Details
A	LYS300-ILE318

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:7899082

Chain	Residue	Details
A	CYS81

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1mht

Chain	Residue	Details
A	CYS81
A	GLU119

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 293

Chain	Residue	Details
A	CYS81	covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor
A	GLU119	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity
A	ARG163	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
A	ARG165	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity

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