CATH Classification
Level | CATH Code | Description |
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3 | Alpha Beta |
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3.30 | 2-Layer Sandwich |
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3.30.470 | D-amino Acid Aminotransferase; Chain A, domain 1 |
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3.30.470.30 | DNA ligase/mRNA capping enzyme |
Domain Context
CATH Clusters
Superfamily | DNA ligase/mRNA capping enzyme |
Functional Family |
Enzyme Information
6.5.1.2 |
DNA ligase (NAD(+)).
based on mapping to UniProt P15042
NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide.
-!- The enzyme, typically found in bacteria, catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by NAD(+), forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.1, EC 6.5.1.6 and EC 6.5.1.7.
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UniProtKB Entries (1)
P15042 |
DNLJ_ECOLI
Escherichia coli K-12
DNA ligase
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PDB Structure
PDB | 4GLX |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structure-guided design, synthesis and biological evaluation of novel DNA ligase inhibitors with in vitro and in vivo anti-staphylococcal activity.
Bioorg.Med.Chem.Lett.
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