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Literature summary extracted from

  • Pascal, J.M.
    DNA and RNA ligases: structural variations and shared mechanisms (2008), Curr. Opin. Struct. Biol., 18, 96-105.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.5.1.1 in complex with the AMP-DNA reaction intermediate Homo sapiens
6.5.1.1 in complex with the AMP-DNA reaction intermediate Pyrococcus furiosus
6.5.1.1 in complex with the AMP-DNA reaction intermediate Saccharolobus solfataricus
6.5.1.2
-
 Escherichia coli
6.5.1.2
-
 Enterococcus faecalis
6.5.1.2
-
 Thermus filiformis

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.1 Homo sapiens
-
-
-
6.5.1.1 Pyrococcus furiosus
-
-
-
6.5.1.1 Saccharolobus solfataricus
-
-
-
6.5.1.2 Enterococcus faecalis
-
-
-
6.5.1.2 Escherichia coli
-
-
-
6.5.1.2 Thermus filiformis
-
-
-

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 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Pyrococcus furiosus AMP + diphosphate + (deoxyribonucleotide)m+n
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Saccharolobus solfataricus AMP + diphosphate + (deoxyribonucleotide)m+n
-
 ?
6.5.1.2 NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m in addition to the unique N-terminal domain Ia that stimulates ligase-AMP formation, there are three C-terminal domains that extend from the OB domain: a small zinc-binding (Zn) domain, a helix-hairpin-helix domain, and a BRCA1 C-terminal domain Escherichia coli AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?
6.5.1.2 NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m in addition to the unique N-terminal domain Ia that stimulates ligase-AMP formation, there are three C-terminal domains that extend from the OB domain: a small zinc-binding (Zn) domain, a helix-hairpin-helix domain, and a BRCA1 C-terminal domain Enterococcus faecalis AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?
6.5.1.2 NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m in addition to the unique N-terminal domain Ia that stimulates ligase-AMP formation, there are three C-terminal domains that extend from the OB domain: a small zinc-binding (Zn) domain, a helix-hairpin-helix domain, and a BRCA1 C-terminal domain Thermus filiformis AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.5.1.1 DNA ligase
-
 Pyrococcus furiosus
6.5.1.1 DNA ligase
-
 Saccharolobus solfataricus
6.5.1.1 DNA ligase I
-
 Homo sapiens
6.5.1.1 LIG1
-
 Homo sapiens
6.5.1.2 DNA ligase
-
 Escherichia coli
6.5.1.2 DNA ligase
-
 Enterococcus faecalis
6.5.1.2 DNA ligase
-
 Thermus filiformis
6.5.1.2 LigA
-
 Escherichia coli
6.5.1.2 LigA
-
 Enterococcus faecalis
6.5.1.2 LigA
-
 Thermus filiformis
6.5.1.2 NAD+-dependent DNA ligase
-
 Escherichia coli
6.5.1.2 NAD+-dependent DNA ligase
-
 Enterococcus faecalis
6.5.1.2 NAD+-dependent DNA ligase
-
 Thermus filiformis

Cofactor

EC Number Cofactor Comment Organism Structure
6.5.1.1 ATP
-
 Homo sapiens
6.5.1.1 ATP
-
 Pyrococcus furiosus
6.5.1.1 ATP
-
 Saccharolobus solfataricus
6.5.1.2 NAD+
-
 Escherichia coli
6.5.1.2 NAD+
-
 Enterococcus faecalis
6.5.1.2 NAD+
-
 Thermus filiformis