CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.3260 | DNA ligase i, domain 1 |
|
1.10.3260.10 | DNA ligase, ATP-dependent, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | DNA ligase, ATP-dependent, N-terminal domain |
| Functional Family | DNA ligase |
Enzyme Information
| 6.5.1.1 |
DNA ligase (ATP).
based on mapping to UniProt P49917
ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate.
-!- The enzyme 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 ATP, 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 6.5.1.2, EC 6.5.1.6 and EC 6.5.1.7.
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UniProtKB Entries (1)
| Q96SD1 |
DCR1C_HUMAN
Homo sapiens
Protein artemis
|
PDB Structure
| PDB | 3W1B |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of the catalytic region of DNA ligase IV in complex with an artemis fragment sheds light on double-strand break repair
Structure
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