eF-site ID 3hfg-A PDB Code 3hfg Chain A Title Crystal Structure of Human 11-beta-hydroxysteroid-dehydrogenase Bound to an Sulfonyl-piperazine Inhibitor Classification OXIDOREDUCTASE Compound Corticosteroid 11-beta-dehydrogenase isozyme 1 Source null (DHI1_HUMAN) Sequence A:  EFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTA RSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQ AGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFL SYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSA SKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMK AVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTT LLIRNPSRKILEFLYSTS Description Functional site 1) chain A residue 121 type sequence I description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 2) chain A residue 124 type sequence T description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 3) chain A residue 125 type sequence S description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 4) chain A residue 126 type sequence L description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 5) chain A residue 170 type sequence S description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 6) chain A residue 171 type sequence L description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 7) chain A residue 172 type sequence A description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 8) chain A residue 177 type sequence Y description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 9) chain A residue 178 type sequence P description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 10) chain A residue 183 type sequence Y description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 11) chain A residue 215 type sequence L description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 12) chain A residue 216 type sequence G description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 13) chain A residue 217 type sequence L description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 14) chain A residue 222 type sequence T description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 15) chain A residue 226 type sequence A description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 16) chain A residue 227 type sequence V description BINDING SITE FOR RESIDUE 17R A 1 source : AC1 17) chain A residue 41 type sequence G description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 18) chain A residue 43 type sequence S description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 19) chain A residue 44 type sequence K description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 20) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 21) chain A residue 46 type sequence I description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 22) chain A residue 65 type sequence A description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 23) chain A residue 66 type sequence R description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 24) chain A residue 67 type sequence S description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 25) chain A residue 92 type sequence T description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 26) chain A residue 93 type sequence M description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 27) chain A residue 119 type sequence N description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 28) chain A residue 120 type sequence H description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 29) chain A residue 121 type sequence I description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 30) chain A residue 168 type sequence V description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 31) chain A residue 169 type sequence S description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 32) chain A residue 170 type sequence S description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 33) chain A residue 183 type sequence Y description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 34) chain A residue 187 type sequence K description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 35) chain A residue 215 type sequence L description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 36) chain A residue 216 type sequence G description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 37) chain A residue 218 type sequence I description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 38) chain A residue 220 type sequence T description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 39) chain A residue 222 type sequence T description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 40) chain A residue 223 type sequence A description BINDING SITE FOR RESIDUE NAP A 293 source : AC2 41) chain A residue 280 type sequence Y description BINDING SITE FOR RESIDUE 17R B 1 source : AC3 42) chain A residue 207 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 43) chain A residue 183 type ACT_SITE sequence Y description Proton acceptor source Swiss-Prot : SWS_FT_FI2 44) chain A residue 170 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15513927, ECO:0007744|PDB:1XU7, ECO:0007744|PDB:1XU9 source Swiss-Prot : SWS_FT_FI4 45) chain A residue 123 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI5 46) chain A residue 162 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI5 47) chain A residue 170-198 type prosite sequence SLAGKVAYPMVAAYSASKFALDGFFSSIR description ADH_SHORT Short-chain dehydrogenases/reductases family signature. SlagkvaypmVaaYSASKFALdGFFsSIR source prosite : PS00061 48) chain A residue 218 type BINDING sequence I description BINDING => ECO:0000269|PubMed:15513927, ECO:0000269|PubMed:17919905, ECO:0000269|PubMed:18069989, ECO:0000269|PubMed:18485702, ECO:0000269|PubMed:18553955, ECO:0000269|PubMed:19217779 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 119 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15513927, ECO:0000269|PubMed:17919905, ECO:0000269|PubMed:18069989, ECO:0000269|PubMed:18485702, ECO:0000269|PubMed:18553955, ECO:0000269|PubMed:19217779 source Swiss-Prot : SWS_FT_FI3 50) chain A residue 183 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15513927, ECO:0000269|PubMed:17919905, ECO:0000269|PubMed:18069989, ECO:0000269|PubMed:18485702, ECO:0000269|PubMed:18553955, ECO:0000269|PubMed:19217779 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 41 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15513927, ECO:0000269|PubMed:17919905, ECO:0000269|PubMed:18069989, ECO:0000269|PubMed:18485702, ECO:0000269|PubMed:18553955, ECO:0000269|PubMed:19217779 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 92 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15513927, ECO:0000269|PubMed:17919905, ECO:0000269|PubMed:18069989, ECO:0000269|PubMed:18485702, ECO:0000269|PubMed:18553955, ECO:0000269|PubMed:19217779 source Swiss-Prot : SWS_FT_FI3

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