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2IH5

Crystal structure of the adenine-specific DNA methyltransferase M.TaqI complexed with the cofactor analog AETA and a 10 bp DNA containing an abasic site analog at the target base partner position

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0006304biological_processDNA modification
A0008168molecular_functionmethyltransferase activity
A0009007molecular_functionsite-specific DNA-methyltransferase (adenine-specific) activity
A0009307biological_processDNA restriction-modification system
A0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NEA A 1001
ChainResidue
AALA47
APHE146
AGOL2001
AHOH2055
AHOH2091
AHOH2116
AHOH2171
AHOH2222
AGLU71
AILE72
AASP73
AALA88
AASP89
APHE90
AASN105
APRO107

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 2001
ChainResidue
AILE119
AVAL121
ATYR129
ALEU142
ANEA1001
AHOH2398

Functional Information from PROSITE/UniProt
site_idPS00092
Number of Residues7
DetailsN6_MTASE N-6 Adenine-specific DNA methylases signature. ILGNPPY
ChainResidueDetails
AILE102-TYR108

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0007744|PDB:2ADM
ChainResidueDetails
ATHR23
AGLU45
AGLU71
AASP89
APRO107

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0007744|PDB:2ADM
ChainResidueDetails
AASN105
ATYR108

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for catalytic activity; via amide nitrogen => ECO:0007744|PDB:2ADM
ChainResidueDetails
APRO106

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 2adm
ChainResidueDetails
APRO106
AASN105
ATYR108

site_idMCSA1
Number of Residues4
DetailsM-CSA 46
ChainResidueDetails
AASN105activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
APRO106activator, electrostatic stabiliser, hydrogen bond acceptor
ATYR108electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
APHE196steric role

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PDB entries from 2024-07-10

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