eF-site ID 3hfg-C PDB Code 3hfg Chain C click to enlarge 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 Homo sapiens (Human) (DHI1_HUMAN) Sequence C:  NEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVV TARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFV AQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVN FLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAY SASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETA MKAVSGIAAPKEECALEIIKGGALRQEEVYYDSSLWTTLL IRNPSRKILEFLYS Description Functional site 1) chain C residue 121 type sequence I description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 2) chain C residue 125 type sequence S description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 3) chain C residue 126 type sequence L description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 4) chain C residue 170 type sequence S description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 5) chain C residue 171 type sequence L description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 6) chain C residue 172 type sequence A description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 7) chain C residue 177 type sequence Y description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 8) chain C residue 178 type sequence P description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 9) chain C residue 183 type sequence Y description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 10) chain C residue 215 type sequence L description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 11) chain C residue 216 type sequence G description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 12) chain C residue 217 type sequence L description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 13) chain C residue 222 type sequence T description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 14) chain C residue 226 type sequence A description BINDING SITE FOR RESIDUE 17R C 1 source : AC5 15) chain C residue 41 type sequence G description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 16) chain C residue 43 type sequence S description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 17) chain C residue 44 type sequence K description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 18) chain C residue 46 type sequence I description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 19) chain C residue 66 type sequence R description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 20) chain C residue 67 type sequence S description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 21) chain C residue 92 type sequence T description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 22) chain C residue 93 type sequence M description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 23) chain C residue 119 type sequence N description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 24) chain C residue 120 type sequence H description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 25) chain C residue 121 type sequence I description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 26) chain C residue 168 type sequence V description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 27) chain C residue 169 type sequence S description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 28) chain C residue 170 type sequence S description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 29) chain C residue 183 type sequence Y description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 30) chain C residue 187 type sequence K description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 31) chain C residue 215 type sequence L description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 32) chain C residue 216 type sequence G description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 33) chain C residue 218 type sequence I description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 34) chain C residue 220 type sequence T description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 35) chain C residue 222 type sequence T description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 36) chain C residue 223 type sequence A description BINDING SITE FOR RESIDUE NAP C 293 source : AC6 37) chain C residue 183 type ACT_SITE sequence Y description Proton acceptor source Swiss-Prot : SWS_FT_FI2 38) chain C 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 39) chain C 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 40) chain C 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 41) chain C 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 42) chain C 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 43) chain C 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 44) chain C residue 123 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI5 45) chain C residue 162 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI5 46) chain C residue 207 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI6

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