Crystal structure of human 20alpha-HSD in ternary complex with NADP and 20alpha-hydroxy-progesterone
The structure was published by Couture, J.F., Legrand, P., Cantin, L., Luu-The, V., Labrie, F., and Breton, R., in 2003 in a paper entitled "Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.59 Å and deposited in 2002.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Aldo-keto reductase family 1 member C1. This molecule has the UniProt identifier Q04828 (AK1C1_HUMAN). The sample contained 323 residues which is 100% of the natural sequence. Out of 323 residues 323 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: