PDBsum entry 2p5n

Oxidoreductase

PDB id: 2p5n

Contents

Protein chains

323 a.a. *

Ligands

NDP ×2

MPD ×2

Waters ×569

* Residue conservation analysis

PDB id:

2p5n

Name:

Oxidoreductase

Title:

Crystal structure of mouse 17-alpha hydroxysteroid dehydrogenase in complex with coenzyme NADPH

Structure:

Aldo-keto reductase family 1, member c21. Chain: a, b. Synonym: 17-alpha hydroxysteroid dehydrogenase, akr1c21. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: akr1c21. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.80Å R-factor: 0.201 R-free: 0.268

Authors:

O.El-Kabbani,U.Dhagat

Key ref:

U.Dhagat et al. (2007). Structure of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) holoenzyme from an orthorhombic crystal form: an insight into the bifunctionality of the enzyme. Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 825-830. PubMed id: 17909281

Date:

15-Mar-07 Release date: 09-Oct-07

Protein chains

Q91WR5  (AK1CL_MOUSE) -  Aldo-keto reductase family 1 member C21 from Mus musculus

Seq: 323 a.a.

Struc: 323 a.a.

Enzyme reactions

• Enzyme class 1: E.C.1.1.1.- - ?????
• Enzyme class 2: E.C.1.1.1.209 - 3(or 17)alpha-hydroxysteroid dehydrogenase.
• Reaction:
  1. androsterone + NADP⁺ = 5alpha-androstan-3,17-dione + NADPH + H⁺
  2. androsterone + NAD⁺ = 5alpha-androstan-3,17-dione + NADH + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Acta Crystallogr Sect F Struct Biol Cryst Commun 63:825-830 (2007)

PubMed id: 17909281

Structure of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) holoenzyme from an orthorhombic crystal form: an insight into the bifunctionality of the enzyme.

U.Dhagat, V.Carbone, R.P.Chung, C.Schulze-Briese, S.Endo, A.Hara, O.El-Kabbani.

ABSTRACT

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.