eF-site ID 2ipg-B PDB Code 2ipg Chain B click to enlarge Title Crystal structure of 17alpha-hydroxysteroid dehydrogenase mutant K31A in complex with NADP+ and epi-testosterone Classification OXIDOREDUCTASE Compound 3(17)alpha-hydroxysteroid dehydrogenase Source (AK1CL_MOUSE) Sequence B:  CHCVILNDGNFIPVLGFGTALPLECPASKAKELTKIAIDA GFHHFDSASVYNTEDHVGEAIRSKIADGTVRREDIFYTSK VWCTSLHPELVRASLERSLQKLQFDYVDLYLIHYPMALKP GEENFPVDEHGKLIFDRVDLCATWEAMEKCKDAGLTKSIG VSNFNYRQLEMILNKPGLKYKPVCNQVECHPYLNQMKLLD FCKSKDIVLVAYGVLGTQRYGGWVDQNSPVLLDEPVLGSM AKKYNRTPALIALRYQLQRGIVVLNTSLKEERIKENMQVF EFQLSSEDMKVLDGLNRNMRYIPAAIFKGHPNWPFLDEY Description Functional site 1) chain B residue 22 type sequence G description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 2) chain B residue 23 type sequence T description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 3) chain B residue 24 type sequence A description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 4) chain B residue 50 type sequence D description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 5) chain B residue 55 type sequence Y description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 6) chain B residue 84 type sequence K description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 7) chain B residue 117 type sequence H description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 8) chain B residue 166 type sequence S description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 9) chain B residue 167 type sequence N description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 10) chain B residue 190 type sequence Q description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 11) chain B residue 216 type sequence Y description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 12) chain B residue 217 type sequence G description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 13) chain B residue 218 type sequence V description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 14) chain B residue 219 type sequence L description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 15) chain B residue 220 type sequence G description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 16) chain B residue 221 type sequence T description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 17) chain B residue 222 type sequence Q description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 18) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 19) chain B residue 236 type sequence L description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 20) chain B residue 253 type sequence A description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 21) chain B residue 269 type sequence N description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 22) chain B residue 270 type sequence T description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 23) chain B residue 271 type sequence S description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 24) chain B residue 272 type sequence L description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 25) chain B residue 273 type sequence K description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 26) chain B residue 276 type sequence R description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 27) chain B residue 279 type sequence E description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 28) chain B residue 280 type sequence N description BINDING SITE FOR RESIDUE NAP B 2 source : AC2 29) chain B residue 25 type sequence L description BINDING SITE FOR RESIDUE FFA B 4 source : AC4 30) chain B residue 27 type sequence L description BINDING SITE FOR RESIDUE FFA B 4 source : AC4 31) chain B residue 55 type sequence Y description BINDING SITE FOR RESIDUE FFA B 4 source : AC4 32) chain B residue 117 type sequence H description BINDING SITE FOR RESIDUE FFA B 4 source : AC4 33) chain B residue 118 type sequence Y description BINDING SITE FOR RESIDUE FFA B 4 source : AC4 34) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE FFA B 4 source : AC4 35) chain B residue 227 type sequence W description BINDING SITE FOR RESIDUE FFA B 4 source : AC4 36) chain B residue 28 type sequence E description BINDING SITE FOR RESIDUE BME B 324 source : AC7 37) chain B residue 29 type sequence C description BINDING SITE FOR RESIDUE BME B 324 source : AC7 38) chain B residue 145 type sequence C description BINDING SITE FOR RESIDUE BME B 325 source : AC8 39) chain B residue 12 type sequence D description BINDING SITE FOR RESIDUE EDO B 326 source : BC1 40) chain B residue 184 type sequence Y description BINDING SITE FOR RESIDUE EDO B 326 source : BC1 41) chain B residue 185 type sequence K description BINDING SITE FOR RESIDUE EDO B 326 source : BC1 42) chain B residue 55 type ACT_SITE sequence Y description Proton donor source Swiss-Prot : SWS_FT_FI1 43) chain B residue 84 type SITE sequence K description Lowers pKa of active site Tyr => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 44) 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 45) 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 46) 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 47) 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 48) 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 49) 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 50) chain B residue 31 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI3 51) chain B residue 117 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3

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