News 2012/5/16 AH-DB now can save search sessions. » more
▼ Go to the search form

AH-DB (Apo and Holo structures DataBase) collects apo and holo structure pairs of proteins. Various protein functions have ben shown directly associated with conformational transitions triggered by binding other molecules. Tertiary structures determined in the unbound and bound state are usually named apo and holo structures, respectively. In AH-DB, we extended the definition of apo and holo structures. The apo strcuture of a protein could be in a apo complex containing other molecules. The corresponding holo strcuture must be in a holo complex containing all the molecules in the corresponding apo complex and some added molecules.

AH-DB is the largest database of apo-holo strcture pairs and provide a sophisticated interface to search and view the collected data. It contains 746314 apo-holo pairs of 3638 proteins from 702 organisms. See more detailed statistics.

Cover
Retrieve a session

Session ID

Recent sessions from your IP

Search sample

The metal-binding loop of copper-zinc superoxide dismutase (SOD1), which destroys free superoxide radicals in the body, has been shown have disorder-to-order transition after binding the ions. Load sample

Organism

AH-DB covers 702 organisms, where the 20 organisms with the most proteins are shown here (detailed statistics). note

Target protein


Ex: KAD_ECOLI, 4AKE:A or adenylate kinase. Multiple keywords with AND/OR operators are allowed. See more detailed usage.

Added molecules










Ex: BAB, amidin, Cu, copper or those in the Target protein field. See more detailed usage. The checkboxs limit added molecules including/excluding the specified molecule types. The option will be ignored if both inclusion and exclusion checkboxes are checked for the same molecule type.

Miscellaneous

, where the note

















(default list)

How to cite AH-DB

Darby Tien-Hao Chang, Tsung-Ju Yao, Chen-Yu Fan, Chih-Yun Chiang and Yi-Han Bai, "AH-DB: collecting protein structure pairs before and after binding", Nucleic Acids Res. 2011.

Mirrors AHDB@NCKU.EE AHDB@NTU.CSBB AHDB@NTU.CSIE