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Literature summary extracted from

  • Cuneo, M.J.; Gabel, S.A.; Krahn, J.M.; Ricker, M.A.; London, R.E.
    The structural basis for partitioning of the XRCC1/DNA ligase III-alpha BRCT-mediated dimer complexes (2011), Nucleic Acids Res., 39, 7816-7827.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.5.1.1 expressed in Escherichia coli BL21-DE3-RIL cells Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.5.1.1 X1BRCTb complexed with L3BRCT Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.1 Homo sapiens P49916
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.5.1.1 immobilized metal affinity column chromatography and Superdex S75 gel filtration Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Homo sapiens AMP + diphosphate + (deoxyribonucleotide)m+n
-
 ?
6.5.1.1 additional information for efficient ligation, ligase III-alpha is constitutively bound to the scaffolding protein XRCC1 through interactions between the C-terminal BRCT domains of each protein Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.5.1.1 homodimer x-ray crystallography Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
6.5.1.1 DNA ligase III
-
 Homo sapiens
6.5.1.1 L3BRCT C-terminal ligase III-alpha BRCT domain Homo sapiens
6.5.1.1 ligase III-alpha
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
6.5.1.1 ATP
-
 Homo sapiens