3vnn Summary

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Crystal Structure of a sub-domain of the nucleotidyltransferase (adenylation) domain of human DNA ligase IV

The structure was published by Ochi, T., Wu, Q., Chirgadze, D.Y., Grossmann, J.G., Bolanos-Garcia, V.M., and Blundell, T.L., in 2012 in a paper entitled "Structural insights into the role of domain flexibility in human DNA ligase IV" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.903 Å and deposited in 2012.

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

The PDB entry contains the structure of DNA ligase 4. This molecule has the UniProt identifier P49917 (DNLI4_HUMAN)search. The sample contained 139 residues which is < 90% of the natural sequence. Out of 139 residues 116 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

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 (268-406) (DNLI4_HUMAN)search Homo sapienssearch < 90% 139 89%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P49917 (268 - 406) DNA ligase 4 Homo sapiens

Chain Sequence family (Pfam)
A ATP dependent DNA ligase domainsearch

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

Chain InterPro annotation
A DNA ligase, ATP-dependent, centralsearch DNA ligase, ATP-dependent, conserved sitesearch DNA ligase 4search