eF-site ID 4fa3-A PDB Code 4fa3 Chain A click to enlarge Title Crystal structure of human 17beta-hydroxysteroid dehydrogenase type 5 in complex with (R)-1-(naphthalen-2-ylsulfonyl)piperidine-3-carboxylic acid (86) Classification OXIDOREDUCTASE/OXIDOREDUCTASE inhibitor Compound Aldo-keto reductase family 1 member C3 Source Homo sapiens (Human) (AK1C3_HUMAN) Sequence A:  QCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAG FRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKL WSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPG IFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMIL NKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYS ALGSQRDKRWVDPNSPVLLEDPVLCALAKKHKRTPALIAL RYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAID GLDRNLHYFNSDSFASHPNYPYSDE Description Functional site 1) chain A residue 22 type sequence G description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 2) chain A residue 23 type sequence T description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 3) chain A residue 24 type sequence Y description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 4) chain A residue 50 type sequence D description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 5) chain A residue 55 type sequence Y description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 6) chain A residue 117 type sequence H description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 7) chain A residue 166 type sequence S description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 8) chain A residue 167 type sequence N description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 9) chain A residue 190 type sequence Q description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 10) chain A residue 216 type sequence Y description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 11) chain A residue 217 type sequence S description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 12) chain A residue 219 type sequence L description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 13) chain A residue 220 type sequence G description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 14) chain A residue 221 type sequence S description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 15) chain A residue 222 type sequence Q description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 16) chain A residue 236 type sequence L description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 17) chain A residue 253 type sequence A description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 18) chain A residue 268 type sequence L description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 19) chain A residue 270 type sequence K description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 20) chain A residue 271 type sequence S description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 21) chain A residue 272 type sequence Y description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 22) chain A residue 276 type sequence R description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 23) chain A residue 279 type sequence Q description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 24) chain A residue 280 type sequence N description BINDING SITE FOR RESIDUE NAP A 401 source : AC1 25) chain A residue 54 type sequence L description BINDING SITE FOR RESIDUE 0SL A 402 source : AC2 26) chain A residue 55 type sequence Y description BINDING SITE FOR RESIDUE 0SL A 402 source : AC2 27) chain A residue 86 type sequence W description BINDING SITE FOR RESIDUE 0SL A 402 source : AC2 28) chain A residue 117 type sequence H description BINDING SITE FOR RESIDUE 0SL A 402 source : AC2 29) chain A residue 167 type sequence N description BINDING SITE FOR RESIDUE 0SL A 402 source : AC2 30) chain A residue 216 type sequence Y description BINDING SITE FOR RESIDUE 0SL A 402 source : AC2 31) chain A residue 227 type sequence W description BINDING SITE FOR RESIDUE 0SL A 402 source : AC2 32) chain A residue 311 type sequence F description BINDING SITE FOR RESIDUE 0SL A 402 source : AC2 33) chain A residue 6 type sequence Q description BINDING SITE FOR RESIDUE EDO A 403 source : AC3 34) chain A residue 17 type sequence P description BINDING SITE FOR RESIDUE EDO A 403 source : AC3 35) chain A residue 18 type sequence V description BINDING SITE FOR RESIDUE EDO A 403 source : AC3 36) chain A residue 19 type sequence L description BINDING SITE FOR RESIDUE EDO A 403 source : AC3 37) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE EDO A 403 source : AC3 38) chain A residue 46 type sequence F description BINDING SITE FOR RESIDUE EDO A 403 source : AC3 39) chain A residue 47 type sequence R description BINDING SITE FOR RESIDUE EDO A 403 source : AC3 40) chain A residue 284 type sequence F description BINDING SITE FOR RESIDUE EDO A 403 source : AC3 41) chain A residue 87 type sequence S description BINDING SITE FOR RESIDUE ACT A 404 source : AC4 42) chain A residue 118 type sequence S description BINDING SITE FOR RESIDUE ACT A 404 source : AC4 43) chain A residue 120 type sequence M description BINDING SITE FOR RESIDUE ACT A 404 source : AC4 44) chain A residue 311 type sequence F description BINDING SITE FOR RESIDUE ACT A 404 source : AC4 45) chain A residue 55 type ACT_SITE sequence Y description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 46) chain A residue 23 type BINDING sequence T description BINDING => ECO:0000269|PubMed:14979715, ECO:0000269|PubMed:14996743, ECO:0000269|PubMed:15087468 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 50 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14979715, ECO:0000269|PubMed:14996743, ECO:0000269|PubMed:15087468 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 166 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14979715, ECO:0000269|PubMed:14996743, ECO:0000269|PubMed:15087468 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 190 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:14979715, ECO:0000269|PubMed:14996743, ECO:0000269|PubMed:15087468 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 216 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:14979715, ECO:0000269|PubMed:14996743, ECO:0000269|PubMed:15087468 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 270 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14979715, ECO:0000269|PubMed:14996743, ECO:0000269|PubMed:15087468 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 276 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14979715, ECO:0000269|PubMed:14996743, ECO:0000269|PubMed:15087468 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 117 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 54) chain A residue 54 type SITE sequence L description Important for substrate specificity => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 84 type SITE sequence K description Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:P14550 source Swiss-Prot : SWS_FT_FI5 56) chain A residue 227 type SITE sequence W description Involved in ligand recognition and product release => ECO:0000269|PubMed:15087468 source Swiss-Prot : SWS_FT_FI6 57) chain A residue 306 type SITE sequence F description Involved in ligand recognition and product release => ECO:0000269|PubMed:15087468 source Swiss-Prot : SWS_FT_FI6 58) chain A residue 151-168 type prosite sequence MEKCKDAGLAKSIGVSNF description ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MekckdaglAKSIGVSNF source prosite : PS00062 59) 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 60) chain A residue 45-62 type prosite sequence GFRHIDSAHLYNNEEQVG description ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GFRHIDSAhlynnEeqVG source prosite : PS00798

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