Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3C58

Crystal structure of a complex between the wild-type lactococcus lactis Fpg (MutM) and a N7-Benzyl-Fapy-dG containing DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003684molecular_functiondamaged DNA binding
A0003690molecular_functiondouble-stranded DNA binding
A0003824molecular_functioncatalytic activity
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006974biological_processDNA damage response
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
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SOS B 7
ChainResidue
APRO1
AARG260
BDT6
BDT8
AGLU2
AGLU5
AMET75
AASN171
AILE172
ASER217
AILE219
ATYR238

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS245
ACYS248
ACYS265
ACYS268

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
ATYR58
AHIS72
AARG74
ATHR113
AGLU115
ATYR125
ALYS129
BDT9
BDT10

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_FI3
Number of Residues1
DetailsActive site: {"description":"Schiff-base intermediate with DNA","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton donor; for beta-elimination activity","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsActive site: {"description":"Proton donor; for delta-elimination activity","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues34
DetailsZinc finger: {"description":"FPG-type"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues28
DetailsRegion: {"description":"DNA-binding"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1k82
ChainResidueDetails
AGLU2
ALYS57
APRO1
AARG260

242199

PDB entries from 2025-09-24

PDB statisticsPDBj update infoContact PDBjnumon