4htp Summary


Crystal structure of the DBD domain of human DNA ligase IV bound to Artemis peptide

The structure was published by De Ioannes, P., Malu, S., Cortes, P., and Aggarwal, A.K., in 2012 in a paper entitled "Structural Basis of DNA Ligase IV-Artemis Interaction in Nonhomologous End-Joining." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2502 Å and deposited in 2012.

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

This PDB entry contains a complex of 2 biomacromolecules, namely DNA ligase 4 and Protein artemis.

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 DNA ligase 4 P49917 (1-240) (DNLI4_HUMAN)search Homo sapienssearch < 90% 240 92%
B DNA ligase 4 P49917 (1-240) (DNLI4_HUMAN)search Homo sapienssearch < 90% 240 92%
C Protein artemis Q96SD1 (485-495) (DCR1C_HUMAN)search Homo sapienssearch < 90% 11 90%
E Protein artemis Q96SD1 (485-495) (DCR1C_HUMAN)search Homo sapienssearch < 90% 11 90%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P49917 (1 - 240) DNA ligase 4 Homo sapiens
Q96SD1 (485 - 495) Protein artemis Homo sapiens

Chain Sequence family (Pfam)
A, B DNA ligase N terminussearch
C, E

Chain ID Molecular function (GO) Biological process (GO)
A, B (P49917) DNA bindingsearch DNA ligase (ATP) activitysearch ATP bindingsearch DNA recombinationsearch DNA repairsearch DNA ligation involved in DNA repairsearch

Chain InterPro annotation
A, B DNA ligase, ATP-dependent, N-terminalsearch DNA ligase 4search
C, E