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

1EE8

CRYSTAL STRUCTURE OF MUTM (FPG) PROTEIN FROM THERMUS THERMOPHILUS HB8

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003684molecular_functiondamaged 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
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003684molecular_functiondamaged DNA binding
B0003824molecular_functioncatalytic activity
B0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
B0006281biological_processDNA repair
B0006284biological_processbase-excision repair
B0006974biological_processDNA damage response
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 501
ChainResidue
ACYS238
ACYS241
ACYS258
ACYS261

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BCYS238
BCYS241
BCYS258
BCYS261

Functional Information from PROSITE/UniProt
site_idPS01242
Number of Residues25
DetailsZF_FPG_1 Zinc finger FPG-type signature. Cpa..CGrpVerrvvag....RGthFCptCQ
ChainResidueDetails
ACYS238-GLN262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues68
DetailsZinc finger: {"description":"FPG-type"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Schiff-base intermediate with DNA","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton donor; for beta-elimination activity","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Proton donor; for delta-elimination activity","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1k82
ChainResidueDetails
AGLU2
ALYS52
APRO1
AARG253

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1k82
ChainResidueDetails
BGLU2
BLYS52
BPRO1
BARG253

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon