Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1MPG

3-METHYLADENINE DNA GLYCOSYLASE II FROM ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003905molecular_functionalkylbase DNA N-glycosylase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006285biological_processbase-excision repair, AP site formation
A0006307biological_processDNA alkylation repair
A0006950biological_processresponse to stress
A0006974biological_processDNA damage response
A0008725molecular_functionDNA-3-methyladenine glycosylase activity
A0016787molecular_functionhydrolase activity
A0032131molecular_functionalkylated DNA binding
A0032993cellular_componentprotein-DNA complex
A0043916molecular_functionDNA-7-methylguanine glycosylase activity
A0052821molecular_functionDNA-7-methyladenine glycosylase activity
A0052822molecular_functionDNA-3-methylguanine glycosylase activity
B0003824molecular_functioncatalytic activity
B0003905molecular_functionalkylbase DNA N-glycosylase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006281biological_processDNA repair
B0006284biological_processbase-excision repair
B0006285biological_processbase-excision repair, AP site formation
B0006307biological_processDNA alkylation repair
B0006950biological_processresponse to stress
B0006974biological_processDNA damage response
B0008725molecular_functionDNA-3-methyladenine glycosylase activity
B0016787molecular_functionhydrolase activity
B0032131molecular_functionalkylated DNA binding
B0032993cellular_componentprotein-DNA complex
B0043916molecular_functionDNA-7-methylguanine glycosylase activity
B0052821molecular_functionDNA-7-methyladenine glycosylase activity
B0052822molecular_functionDNA-3-methylguanine glycosylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 283
ChainResidue
AGLN85
ACYS86
AASN87
AILE90
ATRP263
ATYR266
AHOH306

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 283
ChainResidue
BASN87
BILE90
BVAL91
BTRP263
BTYR266
BHOH380
BGLN85
BCYS86

Functional Information from PROSITE/UniProt
site_idPS00516
Number of Residues25
DetailsALKYLBASE_DNA_GLYCOS Alkylbase DNA glycosidases alkA family signature. GIGrWTAnYFaLrgwqakdvFlpDD
ChainResidueDetails
AGLY214-ASP238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP238
BASP238

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Determinant for substrate specificity and/or activity
ChainResidueDetails
ATRP218
BTRP218

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 313
ChainResidueDetails
ATRP218electrostatic stabiliser, van der waals interaction
ATYR222electrostatic stabiliser, van der waals interaction
AASP238attractive charge-charge interaction, electrostatic stabiliser, promote heterolysis

site_idMCSA2
Number of Residues3
DetailsM-CSA 313
ChainResidueDetails
BTRP218electrostatic stabiliser, van der waals interaction
BTYR222electrostatic stabiliser, van der waals interaction
BASP238attractive charge-charge interaction, electrostatic stabiliser, promote heterolysis

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon