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

6FBU

Crystal structure of the DNA repair enzyme endonuclease-VIII (Nei) from E. coli (E2Q) in complex with AP-site containing DNA substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000703molecular_functionoxidized pyrimidine nucleobase lesion DNA N-glycosylase activity
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
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
A0046872molecular_functionmetal ion binding
A0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 A 301
ChainResidue
AARG8
AASN12
AACT305
AHOH455

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 302
ChainResidue
CPED427
APRO1
AGLU5
AARG212
AHOH493
AHOH502

site_idAC3
Number of Residues1
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG149

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 304
ChainResidue
ACYS237
ACYS240
ACYS257
ACYS260

site_idAC5
Number of Residues2
Detailsbinding site for residue ACT A 305
ChainResidue
AGLU5
ASO4301

Functional Information from PROSITE/UniProt
site_idPS01242
Number of Residues25
DetailsZF_FPG_1 Zinc finger FPG-type signature. Cer..CGsiIekttlss....RPfyWCpgCQ
ChainResidueDetails
ACYS237-GLN261

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsZN_FING: FPG-type
ChainResidueDetails
ALYS228-HIS262

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Schiff-base intermediate with DNA
ChainResidueDetails
APRO1

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AGLN2

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton donor; for beta-elimination activity => ECO:0000305
ChainResidueDetails
ALYS52

site_idSWS_FT_FI5
Number of Residues1
DetailsACT_SITE: Proton donor; for delta-elimination activity => ECO:0000305
ChainResidueDetails
AARG252

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11847126
ChainResidueDetails
AGLN69
AARG124
AASN168

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon