eF-site ID 3fjn-B PDB Code 3fjn Chain B click to enlarge Title The crystal structure of 17-alpha hydroxysteroid dehydrogenase Y224D mutant. Classification OXIDOREDUCTASE Compound Aldo-keto reductase family 1 member C21 Source null (AK1CL_MOUSE) Sequence B:  SKCHCVILNDGNFIPVLGFGTALPLECPKSKAKELTKIAI DAGFHHFDSASVYNTEDHVGEAIRSKIADGTVRREDIFYT SKVWCTSLHPELVRASLERSLQKLQFDYVDLYLIHYPMAL KPGEENFPVDEHGKLIFDRVDLCATWEAMEKCKDAGLTKS IGVSNFNYRQLEMILNKPGLKYKPVCNQVECHPYLNQMKL LDFCKSKDIVLVAYGVLGTQRDGGWVDQNSPVLLDEPVLG SMAKKYNRTPALIALRYQLQRGIVVLNTSLKEERIKENMQ VFEFQLSSEDMKVLDGLNRNMRYIPAAIFKGHPNWPFLDE Y Description Functional site 1) chain B residue 219 type sequence L description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 2) chain B residue 253 type sequence A description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 3) chain B residue 269 type sequence N description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 4) chain B residue 276 type sequence R description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 5) chain B residue 279 type sequence E description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 6) chain B residue 280 type sequence N description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 7) chain B residue 55 type sequence Y description BINDING SITE FOR RESIDUE ACT B 901 source : AC4 8) chain B residue 117 type sequence H description BINDING SITE FOR RESIDUE ACT B 901 source : AC4 9) chain B residue 118 type sequence Y description BINDING SITE FOR RESIDUE ACT B 901 source : AC4 10) chain B residue 167 type sequence N description BINDING SITE FOR RESIDUE ACT B 901 source : AC4 11) chain B residue 216 type sequence Y description BINDING SITE FOR RESIDUE ACT B 901 source : AC4 12) chain B residue 55 type ACT_SITE sequence Y description Proton donor source Swiss-Prot : SWS_FT_FI1 13) chain B residue 84 type SITE sequence K description Lowers pKa of active site Tyr => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 14) 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 15) 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 16) 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 17) 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 18) 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 19) 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 20) chain B residue 31 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 21) chain B residue 117 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3

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