CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.268 | Topoisomerase; domain 3 | |
1.10.268.10 | Topoisomerase, domain 3 |
Domain Context
CATH Clusters
Superfamily | Topoisomerase, domain 3 |
Functional Family | DNA gyrase subunit A |
Enzyme Information
5.6.2.3 |
DNA topoisomerase (ATP-hydrolyzing).
based on mapping to UniProt P72525
ATP-dependent breakage, passage and rejoining of double-stranded DNA.
-!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3.
|
5.6.2.3 |
DNA topoisomerase (ATP-hydrolyzing).
based on mapping to UniProt Q59961
ATP-dependent breakage, passage and rejoining of double-stranded DNA.
-!- The enzyme can introduce negative superhelical turns into double- stranded circular DNA. -!- One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.6.2.2). -!- Formerly EC 5.99.1.3.
|
UniProtKB Entries (1)
P72525 |
PARC_STRPN
Streptococcus pneumoniae TIGR4
DNA topoisomerase 4 subunit A
|
PDB Structure
PDB | 4Z4Q |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structural studies of the drug-stabilized cleavage complexes of topoisomerase IV and gyrase from Streptococcus pneumoniae
To Be Published
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