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1Q39

Crystal structure of the DNA repair enzyme endonuclease-VIII (Nei) from E. coli: The WT enzyme at 2.8 resolution.

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 ZN A 301
ChainResidue
ACYS237
ACYS240
ACYS257
ACYS260

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 302
ChainResidue
AHIS184
AHIS262
AHIS262

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 303
ChainResidue
AHIS220
AASP195
AHIS199

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 304
ChainResidue
AGLU173
ATRP176
ALYS228

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 Residues1
DetailsACT_SITE: Schiff-base intermediate with DNA
ChainResidueDetails
AGLU2

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AGLY3

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor; for beta-elimination activity => ECO:0000305
ChainResidueDetails
AALA53

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton donor; for delta-elimination activity => ECO:0000305
ChainResidueDetails
APRO253

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11847126
ChainResidueDetails
ALEU70
AVAL125
ATYR169

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1k82
ChainResidueDetails
ALYS52
AARG252

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PDB entries from 2024-11-06

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