3a46 Summary


Crystal structure of MvNei1/THF complex

The structure was published by Imamura, K., Wallace, S.S., and Doublie, S., in 2009 in a paper entitled "Structural Characterization of a Viral NEIL1 Ortholog Unliganded and Bound to Abasic Site-containing DNA" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2009.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 3 biomacromolecules, namely Formamidopyrimidine-DNA glycosylase and DNA.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Formamidopyrimidine-DNA glycosylase Q5UQ00 (1-287) (FPG_MIMIV)search Acanthamoeba polyphaga mimivirussearch 100% 289 99%
B Formamidopyrimidine-DNA glycosylase Q5UQ00 (1-287) (FPG_MIMIV)search Acanthamoeba polyphaga mimivirussearch 100% 289 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q5UQ00 (1 - 287) Formamidopyrimidine-DNA glycosylase Acanthamoeba polyphaga mimivirus

Chain Sequence family (Pfam)
A, B (Q5UQ00) PF01149: Formamidopyrimidine-DNA glycosylase N-terminal domainsearch, PF06831: Formamidopyrimidine-DNA glycosylase H2TH domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (Q5UQ00) DNA-(apurinic or apyrimidinic site) lyase activitysearch catalytic activitysearch damaged DNA bindingsearch hydrolase activity, hydrolyzing N-glycosyl compoundssearch zinc ion bindingsearch nucleic acid bindingsearch hydrolase activitysearch oxidized purine nucleobase lesion DNA N-glycosylase activitysearch DNA bindingsearch lyase activitysearch hydrolase activity, acting on glycosyl bondssearch DNA repairsearch metabolic processsearch DNA catabolic process, endonucleolyticsearch base-excision repairsearch cellular response to DNA damage stimulussearch nucleotide-excision repairsearch

Chain InterPro annotation
A, B Ribosomal protein S13-like, H2THsearch DNA glycosylase/AP lyase, catalytic domainsearch DNA glycosylase/AP lyase, H2TH DNA-bindingsearch