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PDBsum entry 2p5n
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Oxidoreductase
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PDB id
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2p5n
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References listed in PDB file
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Key reference
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Title
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Structure of 3(17)alpha-Hydroxysteroid dehydrogenase (akr1c21) holoenzyme from an orthorhombic crystal form: an insight into the bifunctionality of the enzyme.
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Authors
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U.Dhagat,
V.Carbone,
R.P.Chung,
C.Schulze-Briese,
S.Endo,
A.Hara,
O.El-Kabbani.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007,
63,
825-830.
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PubMed id
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Abstract
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Mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) is a bifunctional enzyme
that catalyses the oxidoreduction of the 3- and 17-hydroxy/keto groups of
steroid substrates such as oestrogens, androgens and neurosteroids. The
structure of the AKR1C21-NADPH binary complex was determined from an
orthorhombic crystal belonging to space group P2(1)2(1)2(1) at a resolution of
1.8 A. In order to identify the factors responsible for the bifunctionality of
AKR1C21, three steroid substrates including a 17-keto steroid, a 3-keto steroid
and a 3alpha-hydroxysteroid were docked into the substrate-binding cavity.
Models of the enzyme-coenzyme-substrate complexes suggest that Lys31, Gly225 and
Gly226 are important for ligand recognition and orientation in the active site.
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