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2IBT

Crystal structure of the adenine-specific DNA methyltransferase M.TaqI complexed with the cofactor analog AETA and a 10 bp DNA containing 2-aminopurine at the target position and 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
A0016740molecular_functiontransferase activity
A0032259biological_processmethylation
A0043412biological_processmacromolecule modification
D0003676molecular_functionnucleic acid binding
D0003677molecular_functionDNA binding
D0006304biological_processDNA modification
D0008168molecular_functionmethyltransferase activity
D0009007molecular_functionsite-specific DNA-methyltransferase (adenine-specific) activity
D0009307biological_processDNA restriction-modification system
D0016740molecular_functiontransferase activity
D0032259biological_processmethylation
D0043412biological_processmacromolecule modification
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NEA A 2001
ChainResidue
AVAL21
AASN105
APRO107
APHE146
AGOL3002
AHOH3163
AHOH3189
AHOH3200
AHOH3277
AHOH3305
AALA47
AGLU71
AILE72
AASP73
AALA76
AALA88
AASP89
APHE90

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NEA D 2002
ChainResidue
DVAL21
DALA47
DGLU71
DILE72
DASP73
DALA76
DALA88
DASP89
DPHE90
DASN105
DPRO107
DPHE146
DGOL3003
DHOH3109
DHOH3170
DHOH3243
DHOH3297

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 3001
ChainResidue
AGLU317
AHOH3195
AHOH3313
AHOH3332
AHOH3384
DALA233
DGLU234
DTYR235

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 3002
ChainResidue
ATYR129
ALEU142
ANEA2001
AHOH3273
AHOH3411

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 3003
ChainResidue
DILE72
DTYR129
DLEU142
DNEA2002
DHOH3165
DHOH3359

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 3004
ChainResidue
DARG42
DARG66
DGLU84
DILE86
DPRO95
DHOH3072
DHOH3222

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL D 3005
ChainResidue
AHIS278
APRO279
AGLU321
DPRO81
DGOL3006

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL D 3006
ChainResidue
ALYS277
DARG58
DTHR63
DTYR65
DPHE67
DTRP82
DGOL3005
DHOH3228

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 3007
ChainResidue
ATYR191
ALEU192
AASP219
ATHR220
AGLN221
AGLU222
AARG389
AHOH3034
AHOH3439
AHOH3440

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 Residues10
DetailsBINDING: BINDING => ECO:0007744|PDB:2ADM
ChainResidueDetails
ATHR23
DPRO107
AGLU45
AGLU71
AASP89
APRO107
DTHR23
DGLU45
DGLU71
DASP89

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0007744|PDB:2ADM
ChainResidueDetails
AASN105
ATYR108
DASN105
DTYR108

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for catalytic activity; via amide nitrogen => ECO:0007744|PDB:2ADM
ChainResidueDetails
APRO106
DPRO106

Catalytic Information from CSA
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

site_idMCSA2
Number of Residues4
DetailsM-CSA 46
ChainResidueDetails
DASN105activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
DPRO106activator, electrostatic stabiliser, hydrogen bond acceptor
DTYR108electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
DPHE196steric role

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PDB entries from 2024-04-24

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