1kfv Summary

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Crystal Structure of Lactococcus lactis Formamido-pyrimidine DNA Glycosylase (alias Fpg or MutM) Non Covalently Bound to an AP Site Containing DNA.

The structure was published by Serre, L., Pereira de Jesus, K., Boiteux, S., Zelwer, C., and Castaing, B., in 2002 in a paper entitled "Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.55 Å and deposited in 2001.

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*C)-3', 5'-D(*GP*AP*GP*AP*AP*AP*CP*AP*AP*AP*GP*AP*G)-3', and Formamido-pyrimidine 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 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 Formamido-pyrimidine DNA glycosylase P42371 (2-273) (FPG_LACLC)search Lactococcus lactis subsp. cremorissearch 99% 271 97%
B Formamido-pyrimidine DNA glycosylase P42371 (2-273) (FPG_LACLC)search Lactococcus lactis subsp. cremorissearch 99% 271 97%


This entry contains 1 unique UniProt protein:

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

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (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 N-terminal 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 Biological process (GO) Molecular function (GO)
A, B (P42371) base-excision repairsearch DNA repairsearch nucleotide-excision repairsearch DNA catabolic process, endonucleolyticsearch cellular response to DNA damage stimulussearch metabolic processsearch damaged DNA bindingsearch zinc ion bindingsearch hydrolase activity, hydrolyzing N-glycosyl compoundssearch DNA-(apurinic or apyrimidinic site) lyase activitysearch DNA bindingsearch oxidized purine nucleobase lesion DNA N-glycosylase activitysearch hydrolase activitysearch catalytic activitysearch metal ion bindingsearch nucleic acid bindingsearch lyase activitysearch hydrolase activity, acting on glycosyl bondssearch

Chain InterPro annotation
A, B 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