eF-site ID 3nty-A PDB Code 3nty Chain A click to enlarge Title Crystal structure of AKR1C1 in complex with NADP and 5-Phenyl,3-chlorosalicylic acid Classification OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR Compound Aldo-keto reductase family 1 member C1 Source Homo sapiens (Human) (AK1C1_HUMAN) Sequence A:  QCVKLNDGHFMPVLGFGTYAPAEVPKSKALEATKLAIEAG FRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKL WCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPG EEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGV SNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDF CKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALA KKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFE FQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY Description Functional site 1) chain A residue 22 type sequence G description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 2) chain A residue 23 type sequence T description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 3) chain A residue 24 type sequence Y description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 4) chain A residue 50 type sequence D description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 5) chain A residue 55 type sequence Y description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 6) chain A residue 117 type sequence H description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 7) chain A residue 166 type sequence S description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 8) chain A residue 167 type sequence N description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 9) chain A residue 190 type sequence Q description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 10) chain A residue 216 type sequence Y description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 11) chain A residue 217 type sequence S description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 12) chain A residue 218 type sequence A description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 13) chain A residue 219 type sequence L description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 14) chain A residue 220 type sequence G description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 15) chain A residue 221 type sequence S description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 16) chain A residue 222 type sequence H description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 17) chain A residue 236 type sequence L description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 18) chain A residue 253 type sequence A description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 19) chain A residue 268 type sequence L description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 20) chain A residue 269 type sequence A description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 21) chain A residue 270 type sequence K description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 22) chain A residue 271 type sequence S description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 23) chain A residue 272 type sequence Y description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 24) chain A residue 276 type sequence R description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 25) chain A residue 279 type sequence Q description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 26) chain A residue 280 type sequence N description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 27) chain A residue 306 type sequence L description BINDING SITE FOR RESIDUE NAP A 351 source : AC1 28) chain A residue 24 type sequence Y description BINDING SITE FOR RESIDUE 5P3 A 350 source : AC2 29) chain A residue 54 type sequence L description BINDING SITE FOR RESIDUE 5P3 A 350 source : AC2 30) chain A residue 55 type sequence Y description BINDING SITE FOR RESIDUE 5P3 A 350 source : AC2 31) chain A residue 86 type sequence W description BINDING SITE FOR RESIDUE 5P3 A 350 source : AC2 32) chain A residue 117 type sequence H description BINDING SITE FOR RESIDUE 5P3 A 350 source : AC2 33) chain A residue 222 type sequence H description BINDING SITE FOR RESIDUE 5P3 A 350 source : AC2 34) chain A residue 227 type sequence W description BINDING SITE FOR RESIDUE 5P3 A 350 source : AC2 35) chain A residue 308 type sequence L description BINDING SITE FOR RESIDUE 5P3 A 350 source : AC2 36) chain A residue 133 type sequence E description BINDING SITE FOR RESIDUE ZN A 324 source : AC3 37) chain A residue 248 type sequence H description BINDING SITE FOR RESIDUE ZN A 324 source : AC3 38) chain A residue 292 type sequence E description BINDING SITE FOR RESIDUE ZN A 324 source : AC3 39) chain A residue 50 type catalytic sequence D description 858 source MCSA : MCSA1 40) chain A residue 55 type catalytic sequence Y description 858 source MCSA : MCSA1 41) chain A residue 84 type catalytic sequence K description 858 source MCSA : MCSA1 42) chain A residue 117 type catalytic sequence H description 858 source MCSA : MCSA1 43) chain A residue 55 type ACT_SITE sequence Y description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 117 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 45) chain A residue 54 type SITE sequence L description Important for substrate specificity => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 46) chain A residue 84 type SITE sequence K description Lowers pKa of active site Tyr => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 47) chain A residue 222 type SITE sequence H description May be involved in the mediating step between the transformation of progesterone and the release of the cofactor source Swiss-Prot : SWS_FT_FI7 48) chain A residue 151-168 type prosite sequence VEKCKDAGLAKSIGVSNF description ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. VekckdaglAKSIGVSNF 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 45-62 type prosite sequence GFRHIDSAHLYNNEEQVG description ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GFRHIDSAhlynnEeqVG source prosite : PS00798 51) chain A residue 20 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12899831, ECO:0000269|PubMed:21414777 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 50 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12899831, ECO:0000269|PubMed:21414777 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 166 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12899831, ECO:0000269|PubMed:21414777 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 190 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:12899831, ECO:0000269|PubMed:21414777 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 216 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12899831, ECO:0000269|PubMed:21414777 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 270 type BINDING sequence K description BINDING => ECO:0000269|PubMed:12899831, ECO:0000269|PubMed:21414777 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 24 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 58) chain A residue 222 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 59) chain A residue 227 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3

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