eF-site ID 2he8-B PDB Code 2he8 Chain B click to enlarge Title Crystal structure of 17alpha-hydroxysteroid dehydrogenase in its apo-form Classification OXIDOREDUCTASE Compound Aldo-keto reductase family 1, member C21 Source (Q9CX32_MOUSE) Sequence B:  CHCVILNDGNFIPVLGFGTALPLECPKSKAKELTKIAIDA GFHHFDSASVYNTEDHVGEAIRSKIADGTVRREDIFYTSK VWCTSLHPELVRASLERSLQKLQFDYVDLYLIHYPMALKP GEENFPVDEHGKLIFDRVDLCATWEAMEKCKDAGLTKSIG VSNFNYRQLEMILNKPGLKYKPVCNQVECHPYLNQMKLLD FCKSKDIVLVAYGVLGTQRYGGWVDQNSPVLLDEPVLGSM AKKYNRTPALIALRYQLQRGIVVLNTSLKEERIKENMQVF EFQLSSEDMKVLDGLNRNMRYIPAAIFKGHPNWPFLDEY Description Functional site 1) chain B residue 55 type sequence Y description BINDING SITE FOR RESIDUE ACT A 503 source : AC3 2) chain B residue 28 type sequence E description BINDING SITE FOR RESIDUE BME B 603 source : AC9 3) chain B residue 29 type sequence C description BINDING SITE FOR RESIDUE BME B 603 source : AC9 4) chain B residue 33 type sequence K description BINDING SITE FOR RESIDUE BME B 603 source : AC9 5) chain B residue 219 type sequence L description BINDING SITE FOR RESIDUE GOL B 702 source : BC1 6) chain B residue 269 type sequence N description BINDING SITE FOR RESIDUE GOL B 702 source : BC1 7) chain B residue 270 type sequence T description BINDING SITE FOR RESIDUE GOL B 702 source : BC1 8) chain B residue 271 type sequence S description BINDING SITE FOR RESIDUE GOL B 702 source : BC1 9) chain B residue 276 type sequence R description BINDING SITE FOR RESIDUE GOL B 702 source : BC1 10) chain B residue 279 type sequence E description BINDING SITE FOR RESIDUE GOL B 702 source : BC1 11) chain B residue 280 type sequence N description BINDING SITE FOR RESIDUE GOL B 702 source : BC1 12) chain B residue 55 type ACT_SITE sequence Y description Proton donor source Swiss-Prot : SWS_FT_FI1 13) chain B residue 190 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 216 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 270 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 20 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 50 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 166 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 31 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 20) chain B residue 117 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 21) chain B residue 84 type SITE sequence K description Lowers pKa of active site Tyr => ECO:0000250 source Swiss-Prot : SWS_FT_FI4

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