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1KFV

Crystal Structure of Lactococcus lactis Formamido-pyrimidine DNA Glycosylase (alias Fpg or MutM) Non Covalently Bound to an AP Site Containing DNA.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA 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
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0016829molecular_functionlyase activity
A0019104molecular_functionDNA N-glycosylase activity
A0034039molecular_function8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
A0046872molecular_functionmetal ion binding
A0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA 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
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0016829molecular_functionlyase activity
B0019104molecular_functionDNA N-glycosylase activity
B0034039molecular_function8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
B0046872molecular_functionmetal ion binding
B0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 300
ChainResidue
ACYS245
ACYS248
ACYS265
ACYS268

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BCYS245
BARG247
BCYS248
BCYS265
BCYS268

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
ALEU34
ATYR58
AARG74
ATHR113
AGLU115
ALYS129
AHOH308
DDT9
DDT10

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BLEU34
BTYR58
BARG74
BTHR113
BGLU115
BLYS129
GDT9
GDT10

Functional Information from PROSITE/UniProt
site_idPS01242
Number of Residues25
DetailsZF_FPG_1 Zinc finger FPG-type signature. Csr..CGaeIqkikvag....RGthFCpvCQ
ChainResidueDetails
ACYS245-GLN269

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues68
DetailsZN_FING: FPG-type
ChainResidueDetails
AVAL237-LYS271
BVAL237-LYS271

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with DNA => ECO:0000305
ChainResidueDetails
AGLY1
BGLY1

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AGLU2
BGLU2

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton donor; for beta-elimination activity => ECO:0000305
ChainResidueDetails
ALYS57
BLYS57

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: Proton donor; for delta-elimination activity => ECO:0000305
ChainResidueDetails
AGLY261
BGLY261

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AHIS91
AARG109
BHIS91
BARG109

226707

PDB entries from 2024-10-30

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