CRYSTAL STRUCTURE OF ESCHERICHIA COLI ENDONUCLEASE IV IN COMPLEX WITH DAMAGED DNA
The structure was published by Hosfield, D.J., Guan, Y., Haas, B.J., Cunningham, R.P., and Tainer, J.A., in 1999 in a paper entitled "Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.55 Å and deposited in 1999.
The experimental data on which the structure is based was not deposited.
This entry contains 11 copies of 4 unique biopolymers (complete list).
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 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):
This entry contains 1 unique UniProt protein: