PDBsum entry 1hxh

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protein Protein-protein interface(s) links
Oxidoreductase PDB id
Protein chains
253 a.a. *
Waters ×1256
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Comamonas testosteroni 3beta/17beta hydroxysteroid dehydrogenase
Structure: 3beta/17beta-hydroxysteroid dehydrogenase. Chain: a, b, c, d. Engineered: yes
Source: Comamonas testosteroni. Organism_taxid: 285. Atcc: 11996. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Tetramer (from PQS)
1.22Å     R-factor:   0.146     R-free:   0.180
Authors: J.Benach,C.Filling,U.C.T.Oppermann,P.Roversi,G.Bricogne, K.D.Berndt,H.Jornvall,R.Ladenstein
Key ref:
J.Benach et al. (2002). Structure of bacterial 3beta/17beta-hydroxysteroid dehydrogenase at 1.2 A resolution: a model for multiple steroid recognition. Biochemistry, 41, 14659-14668. PubMed id: 12475215 DOI: 10.1021/bi0203684
15-Jan-01     Release date:   25-Dec-02    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P19871  (3BHD_COMTE) -  3-beta-hydroxysteroid dehydrogenase
254 a.a.
253 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - 3(or 17)-beta-hydroxysteroid dehydrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Testosterone + NAD(P)(+) = androst-4-ene-3,17-dione + NAD(P)H
+ NAD(P)(+)
= androst-4-ene-3,17-dione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   4 terms 
  Biochemical function     oxidoreductase activity     2 terms  


DOI no: 10.1021/bi0203684 Biochemistry 41:14659-14668 (2002)
PubMed id: 12475215  
Structure of bacterial 3beta/17beta-hydroxysteroid dehydrogenase at 1.2 A resolution: a model for multiple steroid recognition.
J.Benach, C.Filling, U.C.Oppermann, P.Roversi, G.Bricogne, K.D.Berndt, H.Jörnvall, R.Ladenstein.
The enzyme 3beta/17beta-hydroxysteroid dehydrogenase (3beta/17beta-HSD) is a steroid-inducible component of the Gram-negative bacterium Comamonas testosteroni. It catalyzes the reversible reduction/dehydrogenation of the oxo/beta-hydroxy groups at positions 3 and 17 of steroid compounds, including hormones and isobile acids. Crystallographic analysis at 1.2 A resolution reveals the enzyme to have nearly identical subunits that form a tetramer with 222 symmetry. This is one of the largest oligomeric structures refined at this resolution. The subunit consists of a monomer with a single-domain structure built around a seven-stranded beta-sheet flanked by six alpha-helices. The active site contains a Ser-Tyr-Lys triad, typical for short-chain dehydrogenases/reductases (SDR). Despite their highly diverse substrate specificities, SDR members show a close to identical folding pattern architectures and a common catalytic mechanism. In contrast to other SDR apostructures determined, the substrate binding loop is well-defined. Analysis of structure-activity relationships of catalytic cleft residues, docking analysis of substrates and inhibitors, and accessible surface analysis explains how 3beta/17beta-HSD accommodates steroid substrates of different conformations.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19102727 Y.Takahashi, G.Moiseyev, K.Farjo, and J.X.Ma (2009).
Characterization of key residues and membrane association domains in retinol dehydrogenase 10.
  Biochem J, 419, 113.  
17298439 X.Wu, S.Knapp, A.Stamp, D.K.Stammers, H.Jörnvall, S.L.Dellaporta, and U.Oppermann (2007).
Biochemical characterization of TASSELSEED 2, an essential plant short-chain dehydrogenase/reductase with broad spectrum activities.
  FEBS J, 274, 1172-1182.  
16783599 L.Miguet, Z.Zhang, M.Barbier, and M.G.Grigorov (2006).
Comparison of a homology model and the crystallographic structure of human 11beta-hydroxysteroid dehydrogenase type 1 (11betaHSD1) in a structure-based identification of inhibitors.
  J Comput Aided Mol Des, 20, 67-81.  
15542590 D.Ogg, B.Elleby, C.Norström, K.Stefansson, L.Abrahmsén, U.Oppermann, and S.Svensson (2005).
The crystal structure of guinea pig 11beta-hydroxysteroid dehydrogenase type 1 provides a model for enzyme-lipid bilayer interactions.
  J Biol Chem, 280, 3789-3794.
PDB code: 1xse
15889412 K.Hirotsu, M.Goto, A.Okamoto, and I.Miyahara (2005).
Dual substrate recognition of aminotransferases.
  Chem Rec, 5, 160-172.  
16244724 M.Cacciarini, V.A.Azov, P.Seiler, H.Künzer, and F.Diederich (2005).
Selective steroid recognition by a partially bridged resorcin[4]arene cavitand.
  Chem Commun (Camb), (), 5269-5271.  
15572774 E.Blanc, P.Roversi, C.Vonrhein, C.Flensburg, S.M.Lea, and G.Bricogne (2004).
Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT.
  Acta Crystallogr D Biol Crystallogr, 60, 2210-2221.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.