eF-site ID 3fjn-AB PDB Code 3fjn Chain A, 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 Mus musculus (Mouse) (AK1CL_MOUSE) Sequence A:  SKCHCVILNDGNFIPVLGFGTALPLECPKSKAKELTKIAI DAGFHHFDSASVYNTEDHVGEAIRSKIADGTVRREDIFYT SKVWCTSLHPELVRASLERSLQKLQFDYVDLYLIHYPMAL KPGEENFPVDEHGKLIFDRVDLCATWEAMEKCKDAGLTKS IGVSNFNYRQLEMILNKPGLKYKPVCNQVECHPYLNQMKL LDFCKSKDIVLVAYGVLGWVDQNSPVLLDEPVLGSMAKKY NRTPALIALRYQLQRGIVVLNTSLKEERIKENMQVFEFQL SSEDMKVLDGLNRNMRYIPAAIFKGHPNWPFLDEY B:  SKCHCVILNDGNFIPVLGFGTALPLECPKSKAKELTKIAI DAGFHHFDSASVYNTEDHVGEAIRSKIADGTVRREDIFYT SKVWCTSLHPELVRASLERSLQKLQFDYVDLYLIHYPMAL KPGEENFPVDEHGKLIFDRVDLCATWEAMEKCKDAGLTKS IGVSNFNYRQLEMILNKPGLKYKPVCNQVECHPYLNQMKL LDFCKSKDIVLVAYGVLGTQRDGGWVDQNSPVLLDEPVLG SMAKKYNRTPALIALRYQLQRGIVVLNTSLKEERIKENMQ VFEFQLSSEDMKVLDGLNRNMRYIPAAIFKGHPNWPFLDE Y Description Functional site 1) chain A residue 55 type sequence Y description BINDING SITE FOR RESIDUE ACT A 601 source : AC1 2) chain A residue 117 type sequence H description BINDING SITE FOR RESIDUE ACT A 601 source : AC1 3) chain A residue 118 type sequence Y description BINDING SITE FOR RESIDUE ACT A 601 source : AC1 4) chain A residue 167 type sequence N description BINDING SITE FOR RESIDUE ACT A 601 source : AC1 5) chain A residue 216 type sequence Y description BINDING SITE FOR RESIDUE ACT A 601 source : AC1 6) chain A residue 103 type sequence L description BINDING SITE FOR RESIDUE ACT A 801 source : AC2 7) chain A residue 107 type sequence Q description BINDING SITE FOR RESIDUE ACT A 801 source : AC2 8) chain A residue 108 type sequence F description BINDING SITE FOR RESIDUE ACT A 801 source : AC2 9) chain A residue 246 type sequence K description BINDING SITE FOR RESIDUE ACT A 801 source : AC2 10) chain B residue 219 type sequence L description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 11) chain B residue 253 type sequence A description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 12) chain B residue 269 type sequence N description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 13) chain B residue 276 type sequence R description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 14) chain B residue 279 type sequence E description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 15) chain B residue 280 type sequence N description BINDING SITE FOR RESIDUE ACT B 701 source : AC3 16) chain B residue 55 type sequence Y description BINDING SITE FOR RESIDUE ACT B 901 source : AC4 17) chain B residue 117 type sequence H description BINDING SITE FOR RESIDUE ACT B 901 source : AC4 18) chain B residue 118 type sequence Y description BINDING SITE FOR RESIDUE ACT B 901 source : AC4 19) chain B residue 167 type sequence N description BINDING SITE FOR RESIDUE ACT B 901 source : AC4 20) chain B residue 216 type sequence Y description BINDING SITE FOR RESIDUE ACT B 901 source : AC4 21) chain A residue 151-168 type prosite sequence MEKCKDAGLTKSIGVSNF description ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MekckdaglTKSIGVSNF source prosite : PS00062 22) chain A residue 55 type ACT_SITE sequence Y description Proton donor source Swiss-Prot : SWS_FT_FI1 23) chain B residue 55 type ACT_SITE sequence Y description Proton donor source Swiss-Prot : SWS_FT_FI1 24) chain A 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 25) 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 26) 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 27) 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 28) chain A 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 29) chain A 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 30) chain A 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 31) chain A 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 32) chain A 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 33) 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 34) 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 35) 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 36) chain A residue 31 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 37) chain A residue 117 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 38) chain B residue 31 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 39) chain B residue 117 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 40) chain A residue 84 type SITE sequence K description Lowers pKa of active site Tyr => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 41) 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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