CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.300 | P-loop containing nucleotide triphosphate hydrolases |
Domain Context
CATH Clusters
| Superfamily | P-loop containing nucleotide triphosphate hydrolases |
| Functional Family | Multidrug ABC transporter ATP-binding protein |
Enzyme Information
| 7.6.2.2 |
ABC-type xenobiotic transporter.
based on mapping to UniProt Q9CHL8
ATP + H(2)O + xenobiotic(Side 1) = ADP + phosphate + xenobiotic(Side 2).
-!- An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. -!- Does not undergo phosphorylation during the transport process. -!- The enzymes from Gram-positive bacteria and eukaryotic cells export a number of drugs with unusual specificity, covering various groups of unrelated substances while ignoring some that are closely related structurally. -!- Several distinct enzymes may be present in a single eukaryotic cell. -!- Many of them also transport glutathione--drug conjugates (see EC 7.6.2.3) while others also show some 'flippase' activity (cf. EC 7.6.2.1). -!- Formerly EC 3.6.3.44.
|
UniProtKB Entries (1)
| Q9CHL8 |
LMRA_LACLA
Lactococcus lactis subsp. lactis Il1403
Multidrug resistance ABC transporter ATP-binding and permease protein
|
PDB Structure
| PDB | 1MV5 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of LmrA ATP-binding domain reveals the two-site alternating mechanism at molecular level
To be Published
|
