eF-site ID 1xjb-B PDB Code 1xjb Chain B click to enlarge Title Crystal structure of human type 3 3alpha-hydroxysteroid dehydrogenase in complex with NADP(H), citrate and acetate molecules Classification OXIDOREDUCTASE Compound Aldo-keto reductase family 1 member C2 Source (AK1C2_HUMAN) Sequence B:  DSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLA IEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFY TSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVS VKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAK SIGVSNFNHRLLEMILNKPGLKYKPVCNQVECHPYFNQRK LLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVL CALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNV QVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSD EY Description Functional site 1) chain B residue 55 type sequence Y description BINDING SITE FOR RESIDUE ACT B 6002 source : AC3 2) chain B residue 117 type sequence H description BINDING SITE FOR RESIDUE ACT B 6002 source : AC3 3) chain B residue 276 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1004 source : AC4 4) chain B residue 91 type sequence R description BINDING SITE FOR RESIDUE SO4 B 5004 source : AC5 5) chain B residue 91 type sequence R description BINDING SITE FOR RESIDUE SO4 B 5004 source : AC5 6) chain B residue 91 type sequence R description BINDING SITE FOR RESIDUE SO4 B 5004 source : AC5 7) chain B residue 22 type sequence G description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 8) chain B residue 23 type sequence T description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 9) chain B residue 24 type sequence Y description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 10) chain B residue 50 type sequence D description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 11) chain B residue 55 type sequence Y description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 12) chain B residue 84 type sequence K description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 13) chain B residue 117 type sequence H description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 14) chain B residue 166 type sequence S description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 15) chain B residue 167 type sequence N description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 16) chain B residue 190 type sequence Q description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 17) chain B residue 216 type sequence Y description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 18) chain B residue 217 type sequence S description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 19) chain B residue 218 type sequence A description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 20) chain B residue 219 type sequence L description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 21) chain B residue 220 type sequence G description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 22) chain B residue 221 type sequence S description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 23) chain B residue 222 type sequence H description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 24) chain B residue 236 type sequence L description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 25) chain B residue 253 type sequence A description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 26) chain B residue 268 type sequence L description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 27) chain B residue 270 type sequence K description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 28) chain B residue 271 type sequence S description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 29) chain B residue 272 type sequence Y description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 30) chain B residue 276 type sequence R description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 31) chain B residue 279 type sequence Q description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 32) chain B residue 280 type sequence N description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 33) chain B residue 306 type sequence L description BINDING SITE FOR RESIDUE NAP B 5001 source : AC7 34) chain B residue 5 type sequence Y description BINDING SITE FOR RESIDUE EDO B 1003 source : AC8 35) chain B residue 6 type sequence Q description BINDING SITE FOR RESIDUE EDO B 1003 source : AC8 36) chain B residue 17 type sequence P description BINDING SITE FOR RESIDUE EDO B 1003 source : AC8 37) chain B residue 18 type sequence V description BINDING SITE FOR RESIDUE EDO B 1003 source : AC8 38) chain B residue 19 type sequence L description BINDING SITE FOR RESIDUE EDO B 1003 source : AC8 39) chain B residue 45 type sequence G description BINDING SITE FOR RESIDUE EDO B 1003 source : AC8 40) chain B residue 46 type sequence F description BINDING SITE FOR RESIDUE EDO B 1003 source : AC8 41) chain B residue 47 type sequence H description BINDING SITE FOR RESIDUE EDO B 1003 source : AC8 42) chain B residue 48 type sequence H description BINDING SITE FOR RESIDUE EDO B 1003 source : AC8 43) chain B residue 284 type sequence F description BINDING SITE FOR RESIDUE EDO B 1003 source : AC8 44) chain B residue 3 type sequence S description BINDING SITE FOR RESIDUE BME A 1005 source : BC2 45) chain B residue 5 type sequence Y description BINDING SITE FOR RESIDUE BME A 1005 source : BC2 46) chain B residue 7 type sequence C description BINDING SITE FOR RESIDUE BME A 1005 source : BC2 47) chain B residue 55 type ACT_SITE sequence Y description Proton donor source Swiss-Prot : SWS_FT_FI1 48) chain B residue 190 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 216 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 270 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338 source Swiss-Prot : SWS_FT_FI2 51) chain B residue 20 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338 source Swiss-Prot : SWS_FT_FI2 52) chain B residue 50 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338 source Swiss-Prot : SWS_FT_FI2 53) chain B residue 166 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11513593, ECO:0000269|PubMed:11514561, ECO:0000269|PubMed:15929998, ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338 source Swiss-Prot : SWS_FT_FI2 54) chain B residue 24 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 55) chain B residue 222 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 56) chain B residue 117 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI4 57) chain B residue 227 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI4 58) chain B residue 84 type SITE sequence K description Lowers pKa of active site Tyr => ECO:0000250 source Swiss-Prot : SWS_FT_FI5

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