1nnj Summary

pdbe.org/1nnj
spacer

Crystal structure Complex between the Lactococcus lactis Fpg and an abasic site containing DNA

The structure was published by Pereira de Jesus, K., Serre, L., Zelwer, C., and Castaing, B., in 2005 in a paper entitled "Structural insights into abasic site for Fpg specific binding and catalysis: comparative high-resolution crystallographic studies of Fpg bound to various models of abasic site analogues-containing DNA." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2003.

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

This PDB entry contains a complex of 3 biomacromolecules, namely 5'-D(*CP*TP*CP*TP*TP*TP*(PDI)P*TP*TP*TP*CP*TP*CP*G)-3', 5'-D(*GP*CP*GP*AP*GP*AP*AP*AP*CP*AP*AP*AP*GP*A)-3', and Formamidopyrimidine-DNA glycosylase.

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 most likely forms heterotrimers.

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 P42371 (2-273) (FPG_LACLC)search Lactococcus lactis subsp. cremorissearch 99% 271 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P42371 (2 - 273) Formamidopyrimidine-DNA glycosylase Lactococcus lactis

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P42371) Middle domain of MutM-like DNA repair proteinssearch, N-terminal domain of MutM-like DNA repair proteinssearch, C-terminal, Zn-finger domain of MutM-like DNA repair proteinssearch Helicase, Ruva Protein; domain 3search PF01149: Formamidopyrimidine-DNA glycosylase N-terminal domainsearch, PF06827: Zinc finger found in FPG and IleRSsearch, PF06831: Formamidopyrimidine-DNA glycosylase H2TH domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A (P42371) lyase activitysearch hydrolase activitysearch DNA-(apurinic or apyrimidinic site) lyase activitysearch metal ion bindingsearch oxidized purine nucleobase lesion DNA N-glycosylase activitysearch zinc ion bindingsearch hydrolase activity, acting on glycosyl bondssearch DNA bindingsearch catalytic activitysearch DNA catabolic process, endonucleolyticsearch DNA repairsearch cellular response to DNA damage stimulussearch metabolic processsearch

Chain InterPro annotation
A DNA glycosylase/AP lyasesearch Zinc finger, DNA glycosylase/AP lyase-typesearch Zinc finger, DNA glycosylase/AP lyase/isoleucyl tRNA synthetasesearch Ribosomal protein S13-like, H2THsearch DNA glycosylase/AP lyase, catalytic domainsearch DNA glycosylase/AP lyase, H2TH DNA-bindingsearch DNA glycosylase/AP lyase, zinc finger domain, DNA-binding sitesearch Formamidopyrimidine-DNA glycosylasesearch