eF-site ID 1xjb-A PDB Code 1xjb Chain A 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 A:  SVDDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAV KLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKRED IFYTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHF PVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAG LAKSIGVSNFNHRLLEMILNKPGLKYKPVCNQVECHPYFN QRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLED PVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIR QNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYP FSDEY Description Functional site 1) chain A residue 6 type sequence Q description BINDING SITE FOR RESIDUE ACT A 1002 source : AC1 2) chain A residue 17 type sequence P description BINDING SITE FOR RESIDUE ACT A 1002 source : AC1 3) chain A residue 18 type sequence V description BINDING SITE FOR RESIDUE ACT A 1002 source : AC1 4) chain A residue 19 type sequence L description BINDING SITE FOR RESIDUE ACT A 1002 source : AC1 5) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE ACT A 1002 source : AC1 6) chain A residue 47 type sequence H description BINDING SITE FOR RESIDUE ACT A 1002 source : AC1 7) chain A residue 284 type sequence F description BINDING SITE FOR RESIDUE ACT A 1002 source : AC1 8) chain A residue 55 type sequence Y description BINDING SITE FOR RESIDUE ACT A 5002 source : AC2 9) chain A residue 117 type sequence H description BINDING SITE FOR RESIDUE ACT A 5002 source : AC2 10) chain A residue 96 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1004 source : AC4 11) chain A residue 22 type sequence G description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 12) chain A residue 23 type sequence T description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 13) chain A residue 24 type sequence Y description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 14) chain A residue 50 type sequence D description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 15) chain A residue 55 type sequence Y description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 16) chain A residue 84 type sequence K description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 17) chain A residue 117 type sequence H description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 18) chain A residue 166 type sequence S description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 19) chain A residue 167 type sequence N description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 20) chain A residue 190 type sequence Q description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 21) chain A residue 216 type sequence Y description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 22) chain A residue 217 type sequence S description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 23) chain A residue 218 type sequence A description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 24) chain A residue 219 type sequence L description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 25) chain A residue 220 type sequence G description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 26) chain A residue 221 type sequence S description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 27) chain A residue 222 type sequence H description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 28) chain A residue 236 type sequence L description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 29) chain A residue 253 type sequence A description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 30) chain A residue 268 type sequence L description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 31) chain A residue 269 type sequence A description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 32) chain A residue 270 type sequence K description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 33) chain A residue 271 type sequence S description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 34) chain A residue 272 type sequence Y description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 35) chain A residue 276 type sequence R description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 36) chain A residue 279 type sequence Q description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 37) chain A residue 280 type sequence N description BINDING SITE FOR RESIDUE NAP A 1001 source : AC6 38) chain A residue 123 type sequence K description BINDING SITE FOR RESIDUE EDO A 5003 source : AC9 39) chain A residue 140 type sequence D description BINDING SITE FOR RESIDUE EDO A 5003 source : AC9 40) chain A residue 141 type sequence T description BINDING SITE FOR RESIDUE EDO A 5003 source : AC9 41) chain A residue 24 type sequence Y description BINDING SITE FOR RESIDUE CIT A 1006 source : BC1 42) chain A residue 54 type sequence V description BINDING SITE FOR RESIDUE CIT A 1006 source : BC1 43) chain A residue 86 type sequence W description BINDING SITE FOR RESIDUE CIT A 1006 source : BC1 44) chain A residue 222 type sequence H description BINDING SITE FOR RESIDUE CIT A 1006 source : BC1 45) chain A residue 227 type sequence W description BINDING SITE FOR RESIDUE CIT A 1006 source : BC1 46) chain A residue 306 type sequence L description BINDING SITE FOR RESIDUE CIT A 1006 source : BC1 47) chain A residue 5 type sequence Y description BINDING SITE FOR RESIDUE BME A 1005 source : BC2 48) chain A residue 151-168 type prosite sequence MEKCKDAGLAKSIGVSNF description ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MekckdaglAKSIGVSNF source prosite : PS00062 49) chain A residue 268-283 type prosite sequence LAKSYNEQRIRQNVQV description ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LAKSYNeqRIrQNvQV source prosite : PS00063 50) chain A residue 55 type ACT_SITE sequence Y description Proton donor source Swiss-Prot : SWS_FT_FI1 51) chain A 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 A 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 A 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 A 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 55) chain A 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 56) chain A 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 57) chain A residue 24 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 58) chain A residue 222 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 59) chain A residue 117 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI4 60) chain A residue 227 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI4 61) chain A 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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