3a42 Summary

pdbe.org/3a42
spacer

Crystal structure of MvNei1

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 2.6 Å and deposited in 2009.

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

The PDB entry contains the structure of Formamidopyrimidine-DNA glycosylase. This molecule has the UniProt identifier Q5UQ00 (FPG_MIMIV)search. The sample contained 295 residues which is 100% of the natural sequence. Out of 295 residues 282 were observed and are deposited in the PDB.

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 is most likely monomeric.

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% 295 95%


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 (Q5UQ00) PF01149: Formamidopyrimidine-DNA glycosylase N-terminal domainsearch, PF06831: Formamidopyrimidine-DNA glycosylase H2TH domainsearch

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

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