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3TWK

Crystal structure of arabidopsis thaliana FPG

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003684molecular_functiondamaged DNA binding
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0008270molecular_functionzinc ion binding
A0008534molecular_functionoxidized purine nucleobase lesion DNA N-glycosylase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0019104molecular_functionDNA N-glycosylase activity
B0003676molecular_functionnucleic acid binding
B0003684molecular_functiondamaged DNA binding
B0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
B0006281biological_processDNA repair
B0006284biological_processbase-excision repair
B0008270molecular_functionzinc ion binding
B0008534molecular_functionoxidized purine nucleobase lesion DNA N-glycosylase activity
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0019104molecular_functionDNA N-glycosylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
APRO2
AMSE78
AHOH468

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AHOH607
ASER68
ASER205
ASER206
ALEU207
ASER208
AHOH606

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with DNA => ECO:0000255|PROSITE-ProRule:PRU00392
ChainResidueDetails
APRO2
BPRO2

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU00392
ChainResidueDetails
AGLU3
BGLU3

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor; for beta-elimination activity => ECO:0000255|PROSITE-ProRule:PRU00392
ChainResidueDetails
ALYS60
BLYS60

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22789755
ChainResidueDetails
ATYR107
ALYS167
AASN186
BTYR107
BLYS167
BASN186

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG126
BARG126

222624

PDB entries from 2024-07-17

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