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

1DIZ

CRYSTAL STRUCTURE OF E. COLI 3-METHYLADENINE DNA GLYCOSYLASE (ALKA) COMPLEXED WITH DNA

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 Residues5
DetailsBINDING SITE FOR RESIDUE NA B 824
ChainResidue
BGLN210
BPHE212
BILE215
BHOH844
CDC11

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 825
ChainResidue
EDC11
AGLN210
APHE212
AILE215
AHOH850

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_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10946229, 10675345
ChainResidueDetails
ATRP272
AASP238
ATYR222

site_idCSA2
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10946229, 10675345
ChainResidueDetails
BTRP272
BASP238
BTYR222

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon