| General information | | DisProt: | DP00690 | | Name: | Aldo-keto reductase family 1 member C21 | | Synonym(s): | AK1CL_MOUSE
17-alpha-hydroxysteroid dehydrogenase Short name=17-alpha-HSD
3-alpha-hydroxysteroid dehydrogenase
Dihydrodiol dehydrogenase type 1 Short name=DD1
Dihydrodiol dehydrogenase type 3 Short name=DD3
| | First appeared in release: | Release 5.1 (05/28/2010) | | UniProt: | Q91WR5 | | UniGene: | Mm.27085 | | SwissProt: | AK1CL_MOUSE | | TrEMBL: | | | NCBI (GI): | 172045824 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 323 | | Percent disordered: | 2% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MNSKCHCVIL NDGNFIPVLG FGTALPLECP KSKAKELTKI AIDAGFHHFD SASVYNTEDH - 60
VGEAIRSKIA DGTVRREDIF YTSKVWCTSL HPELVRASLE RSLQKLQFDY VDLYLIHYPM - 120
ALKPGEENFP VDEHGKLIFD RVDLCATWEA MEKCKDAGLT KSIGVSNFNY RQLEMILNKP - 180
GLKYKPVCNQ VECHPYLNQM KLLDFCKSKD IVLVAYGVLG TQRYGGWVDQ NSPVLLDEPV - 240
LGSMAKKYNR TPALIALRYQ LQRGIVVLNT SLKEERIKEN MQVFEFQLSS EDMKVLDGLN - 300
RNMRYIPAAI FKGHPNWPFL DEY
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| Functional narrative |
NADP-dependent 17-alpha-hydroxysteroid dehydrogenase that converts 5-alpha-androstane-3,17-dione into epitestosterone. Has lower 3-alpha-hydroxysteroid dehydrogenase activity. Has broad substrate specificity and acts on various 17-alpha-hydroxysteroids, 17-ketosteroids, 3-alpha hydroxysteroids and 3-ketosteroids. Reduction of keto groups is strictly stereoselective. Reduction of 17-ketosteroids yields only 17-alpha-hydroxysteroids. Likewise, reduction of 3-ketosteroids yields only 3-alpha-hydroxysteroids
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | Loop B | | Location: | 222 - 226 | | Length: | 5 | | Region sequence: |
QRDGG | | Modification type: | Mutant
| | PDB: | 3FJN:A, 3FJN:B | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | Substrate/ligand binding
| Detection methods:
- X-ray crystallography (100 K; ethylene glycol 20 %; magnesium acetate (buffer) 0.3 M; PEG 8000 (buffer) 20 %; sodium cacodylate (buffer) 0.1 M)
| References:
- Dhagat U, Endo S, Mamiya H, Hara A, El-Kabbani O. "Studies on a Tyr residue critical for the binding of coenzyme and substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21): structure of the Y224D mutant enzyme." Acta Crystallogr D Biol Crystallogr. 2010; 66(Pt 2): 198-204. PubMed: 20124700
| Comments:Disordered region contains Y-->D mutation at aa position 224.
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