CATH Classification

Domain Context

CATH Clusters

Superfamily P-loop containing nucleotide triphosphate hydrolases
Functional Family Cystic fibrosis transmembrane conductance regulator

Enzyme Information

5.6.1.6
Channel-conductance-controlling ATPase.
based on mapping to UniProt P13569
ATP + H(2)O + closed Cl(-) channel = ADP + phosphate + open Cl(-) channel.
-!- ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. -!- The enzyme is found in animals, and in humans its absence brings about cystic fibrosis. -!- Unlike most of the ABC transporters, chloride pumping is not directly coupled to ATP hydrolysis. -!- Instead, the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains. -!- The enzyme is also involved in the functioning of other transmembrane channels. -!- Formerly EC 3.6.3.49.
7.5.2.1
ABC-type maltose transporter.
based on mapping to UniProt P68187
ATP + H(2)O + maltose-[maltose-binding protein](Side 1) = ADP + phosphate + maltose(Side 2) + [maltose-binding protein](Side 1).
-!- An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. -!- The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of maltose and maltose oligosaccharides. -!- Formerly EC 3.6.3.19.

UniProtKB Entries (2)

P68187
MALK_ECOLI
Escherichia coli K-12
Maltose/maltodextrin import ATP-binding protein MalK
P13569
CFTR_HUMAN
Homo sapiens
Cystic fibrosis transmembrane conductance regulator

PDB Structure

PDB 3GD7
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of human NBD2 complexed with N6-Phenylethyl-ATP (P-ATP)
Atwell, S., Antonysamy, S., Guggino, W.B., Conners, K., Emtage, S., Gheyi, T., Hunt, J.F., Lewis, H.A., Lu, F., Sauder, J.M., Weber, P.C., Wetmore, D., Zhao, X.
To be Published
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