1ckq Summary



A publication describing this structure is not available. The depositing authors are Horvath, M.search; Rosenberg, J.M.search

This crystal structure was determined using X-ray diffraction at a resolution of 1.85 Å and deposited in 1999.

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

This PDB entry contains a complex of 2 biomacromolecules, namely DNA (5'-D(*TP*CP*GP*CP*GP*AP*AP*TP*TP*CP*GP*CP*G)-3') and PROTEIN (ENDONUCLEASE).

The molecule most likely forms heterotetramers.

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 PROTEIN (ENDONUCLEASE) P00642 (2-277) (T2E1_ECOLX)search Escherichia colisearch 94% 276 94%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00642 (2 - 277) PROTEIN (ENDONUCLEASE) Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00642) Restriction endonuclease EcoRIsearch Eco RI Endonuclease, subunit Asearch PF02963: Restriction endonuclease EcoRIsearch

Chain ID Molecular function (GO) Biological process (GO)
A (P00642) DNA bindingsearch magnesium ion bindingsearch Type II site-specific deoxyribonuclease activitysearch hydrolase activitysearch endonuclease activitysearch nuclease activitysearch metal ion bindingsearch DNA restriction-modification systemsearch DNA catabolic process, endonucleolyticsearch nucleic acid phosphodiester bond hydrolysissearch

Chain InterPro annotation
A Restriction endonuclease, type II, EcoRIsearch Restriction endonuclease type II-likesearch Restriction endonuclease, type II, EcoRI/MunIsearch Restriction endonuclease, type II, EcoRI, Proteobacteriasearch