eF-site ID 6q9e-.a1.a2.a3.a4.b1.b2.c1.c2.d1.d2.f1.f2.h1.h2.i1.i2.q1.q2.x1.x2 PDB Code 6q9e Chain a1, a2, a3, a4, b1, b2, c1, c2, d1, d2, f1, f2, h1, h2, i1, i2, q1, q2, x1, x2 Title Complex III2 focused refinement from Ovine respiratory supercomplex I+III2 Classification ELECTRON TRANSPORT Compound Ubiquinol-cytochrome c reductase core protein 1 Source ORGANISM_COMMON: Sheep; ORGANISM_SCIENTIFIC: Ovis aries; Sequence a1:  ATYAQALQSVPETQVSQLDNGLRVASEQSSQPTCTVGVWI DAGSRYETEKNNGAGYFVEHLAFKGTKNRPGNALEKEVES MGAHLNAYSTREHTAYYIKALSKDLPKAVELLADIVQNCS LEDSQIEKERDVILQELQENDTSMRDVVFNYLHATAFQGT PLAQSVEGPSENVRKLSRADLTEYLSRHYKAPRMVLAAAG GLEHRQLLDLAQKHFSGLSGTPTLTPCRFTGSEIRHREDG LPLAHVAIAVEGPGWANPDNVALQVANAIIGHYDCTYGGG MHLSSPLASVAVTNKLCQSFQTFNICYADTGLLGAHFVCD HMSIDDMMFVLQGQWMRLCTSATESEVVRGKNLLRNALVS HLDGTTPVCEDIGRSLLTYGRRIPLAEWESRIAEVDARVV REVCSKYFYDQCPAVAGFGPIEQLPDYNRIRSGMFWLRF a2:  HPQDLEFTRLPNGLVIASLENYAPASRIGLFIKAGSRYEN FNNLGTSHLLRLASSLTTKGASSFKITRGIEAVGGKLSVT STRENMAYTVECLRDDVDILMEFLLNVTTAPEFRRWEVAA LQSQLRIDKAVAFQNPQAHVIENLHAAAYRNALANSLYCP DYRIGKVTPDELHDYVQNHFTSARMALIGLGVSHPVLKQV AEQFLNIRGAKAKYRGGEIREQNGDSLVHAALVAESAAIG SAEANAFSVLQHVLGAGPHVKRGSNATSSLYQAVAKGVHQ PFDVSAFNASYSDSGLFGFYTISQAASAGDVIKAAYNQVK TIAQGNLSNPDVQAAKNKLKAGYLMSVESSEGFLDEVGCQ ALAAGSYTPPSTVLQQIDAVADADVINAAKKFVSGRKSMA ASGNLGHTPFIDEL a3:  ATYAQALQSVPETQVSQLDNGLRVASEQSSQPTCTVGVWI DAGSRYETEKNNGAGYFVEHLAFKGTKNRPGNALEKEVES MGAHLNAYSTREHTAYYIKALSKDLPKAVELLADIVQNCS LEDSQIEKERDVILQELQENDTSMRDVVFNYLHATAFQGT PLAQSVEGPSENVRKLSRADLTEYLSRHYKAPRMVLAAAG GLEHRQLLDLAQKHFSGLSGTYDEDAVPTLTPCRFTGSEI RHREDGLPLAHVAIAVEGPGWANPDNVALQVANAIIGHYD CTYGGGMHLSSPLASVAVTNKLCQSFQTFNICYADTGLLG AHFVCDHMSIDDMMFVLQGQWMRLCTSATESEVVRGKNLL RNALVSHLDGTTPVCEDIGRSLLTYGRRIPLAEWESRIAE VDARVVREVCSKYFYDQCPAVAGFGPIEQLPDYNRIRSGM FWLR a4:  HPQDLEFTRLPNGLVIASLENYAPASRIGLFIKAGSRYEN FNNLGTSHLLRLASSLTTKGASSFKITRGIEAVGGKLSVT STRENMAYTVECLRDDVDILMEFLLNVTTAPEFRRWEVAA LQSQLRIDKAVAFQNPQAHVIENLHAAAYRNALANSLYCP DYRIGKVTPDELHDYVQNHFTSARMALIGLGVSHPVLKQV AEQFLNIRAKAKYRGGEIREQNGDSLVHAALVAESAAIGS AEANAFSVLQHVLGAGPHVKRGSNATSSLYQAVAKGVHQP FDVSAFNASYSDSGLFGFYTISQAASAGDVIKAAYNQVKT IAQGNLSNPDVQAAKNKLKAGYLMSVESSEGFLDEVGCQA LAAGSYTPPSTVLQQIDAVADADVINAAKKFVSGRKSMAA SGNLGHTPFIDEL b1:  INIRKTHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICL ILQILTGLFLAMHYTPDTTTAFSSVTHICRDVNYGWIIRY MHANGASMFFICLFMHVGRGLYYGSYTFLETWNIGVILLF ATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLV EWIWGGFSVDKATLTRFFAFHFIFPFIIAALAMVHLLFLH ETGSNNPTGIPSDTDKIPFHPYYTIKDILGAILLILILML LVLFTPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAIL RSIPNKLGGVLALVLSILVLVIMPLLHTSKQRSMMFRPIS QCMFWILVADLLTLTWIGGQPVEHPYIIIGQLASIMYFLI ILVMMPVASIIENNLLKW b2:  INIRKTHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICL ILQILTGLFLAMHYTPDTTTAFSSVTHICRDVNYGWIIRY MHANGASMFFICLFMHVGRGLYYGSYTFLETWNIGVILLF ATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLV EWIWGGFSVDKATLTRFFAFHFIFPFIIAALAMVHLLFLH ETGSNNPTGIPSDTDKIPFHPYYTIKDILGAILLILILML LVLFTPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAIL RSIPNKLGGVLALVLSILVLVIMPLLHTSKQRSMMFRPIS QCMFWILVADLLTLTWIGGQPVEHPYIIIGQLASIMYFLI ILVMMPVASIIENNLLKW c1:  SDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCSSC HSMDYVAYRHLVGVCYTEDEAKALAEEVEVQDGPNEDGEM FMRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRAR HGGEDYVFSLLTGYCEPPRVSLREGLYFNPYFPGQAIGMA PPIYNEVLEFDDGTPATMSQVAKDVCTFLRWAAEPEHDHR KRMGLKMLLMMGLLLPLVYAMKRHKWSVLKSRKLAYRPP c2:  DLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCSSCH SMDYVAYRHLVGVCYTEDEAKALAEEVEVQDGPNEDGEMF MRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRARH GGEDYVFSLLTGYCEPPRVSLREGLYFNPYFPGQAIGMAP PIYNEVLEFDDGTPATMSQVAKDVCTFLRWAAEPEHDHRK RMGLKMLLMMGLLLPLVYAMKRHKWSVLKSRKLAYRPP d1:  KWLEGIRKWYYNAAGFNKLGLMRDDTIHENDDVKEAIRRL PENLYNDRVFRIKRALDLSMRQQILPKEQWTKYEEDKFYL EPYLKEVIRERKEREEWTKK d2:  SSKWLEGIRKWYYNAAGFNKLGLMRDDTIHENDDVKEAIR RLPENLYNDRVFRIKRALDLSMRQQILPKEQWTKYEEDKF YLEPYLKEVIRERKEREEWTK f1:  SHTDIKVPDFSDYRRPEVLDSTKSSKESSEARKGFSYLIT ATTTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSD IPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDP QHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPC HGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG f2:  HTDIKVPDFSDYRRPEVLDSTKSSKESSEARKGFSYLITA TTTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSDI PEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDPQ HDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCH GSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG h1:  LVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSQTEE DCTEELFDFLHARDHCVAHKLFNSL h2:  LVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSQTEE DCTEELFDFLHARDHCVAHKLFNSL i1:  LTARLYSLLFRRTSTFALTIVVGALFFERAFDQGADAIYE HINEGKLWKHIKHKY i2:  PTLTARLYSLLFRRTSTFALTIVVGALFFERAFDQGADAI YEHINEGKLWKHIKHKY q1:  GRQFGHLTRVRHVITYSLSPFEQRAFPHYFSKGIPNVLRR TRACILRVAPPFVVFYLVYTWGTQEFEKSKRKN q2:  RQFGHLTRVRHVITYSLSPFEQRAFPHYFSKGIPNVLRRT RACILRVAPPFVVFYLVYTWGTQEFEKSKRKNPAA x1:  XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX x2:  XXXXXXXXXXXXXXXXXXXXXXXXXXXXXX Description (1)  Ubiquinol-cytochrome c reductase core protein 1, Ubiquinol-cytochrome c reductase core protein 2, Cytochrome b, Cytochrome c1, Cytochrome b-c1 complex subunit Rieske, mitochondrial (E.C.1.10.2.2), Cytochrome b-c1 complex subunit 7, Ubiquinol-cytochrome c reductase complex III subunit VII, Cytochrome b-c1 complex subunit 6, Ubiquinol-cytochrome c reductase, complex III subunit X Functional site 1) chain b1 residue 48 type sequence G description binding site for residue HEM b1 401 source : AC1 2) chain b1 residue 52 type sequence A description binding site for residue HEM b1 401 source : AC1 3) chain b1 residue 80 type sequence R description binding site for residue HEM b1 401 source : AC1 4) chain b1 residue 83 type sequence H description binding site for residue HEM b1 401 source : AC1 5) chain b1 residue 87 type sequence A description binding site for residue HEM b1 401 source : AC1 6) chain b1 residue 90 type sequence F description binding site for residue HEM b1 401 source : AC1 7) chain b1 residue 130 type sequence G description binding site for residue HEM b1 401 source : AC1 8) chain b1 residue 134 type sequence P description binding site for residue HEM b1 401 source : AC1 9) chain b1 residue 182 type sequence H description binding site for residue HEM b1 401 source : AC1 10) chain b1 residue 183 type sequence F description binding site for residue HEM b1 401 source : AC1 11) chain b1 residue 186 type sequence P description binding site for residue HEM b1 401 source : AC1 12) chain b1 residue 31 type sequence W description binding site for residue HEM b1 402 source : AC2 13) chain b1 residue 34 type sequence G description binding site for residue HEM b1 402 source : AC2 14) chain b1 residue 97 type sequence H description binding site for residue HEM b1 402 source : AC2 15) chain b1 residue 98 type sequence V description binding site for residue HEM b1 402 source : AC2 16) chain b1 residue 100 type sequence R description binding site for residue HEM b1 402 source : AC2 17) chain b1 residue 113 type sequence W description binding site for residue HEM b1 402 source : AC2 18) chain b1 residue 116 type sequence G description binding site for residue HEM b1 402 source : AC2 19) chain b1 residue 117 type sequence V description binding site for residue HEM b1 402 source : AC2 20) chain b1 residue 119 type sequence L description binding site for residue HEM b1 402 source : AC2 21) chain b1 residue 196 type sequence H description binding site for residue HEM b1 402 source : AC2 22) chain b1 residue 200 type sequence L description binding site for residue HEM b1 402 source : AC2 23) chain b1 residue 205 type sequence S description binding site for residue HEM b1 402 source : AC2 24) chain b1 residue 206 type sequence N description binding site for residue HEM b1 402 source : AC2 25) chain b1 residue 30 type sequence W description binding site for residue 3PE b1 403 source : AC3 26) chain b1 residue 95 type sequence F description binding site for residue 3PE b1 403 source : AC3 27) chain b1 residue 96 type sequence M description binding site for residue 3PE b1 403 source : AC3 28) chain b1 residue 103 type sequence Y description binding site for residue 3PE b1 403 source : AC3 29) chain b1 residue 104 type sequence Y description binding site for residue 3PE b1 403 source : AC3 30) chain b1 residue 276 type sequence F description binding site for residue 3PE b1 403 source : AC3 31) chain b1 residue 316 type sequence M description binding site for residue 3PE b1 403 source : AC3 32) chain b1 residue 326 type sequence W description binding site for residue 3PE b1 403 source : AC3 33) chain b1 residue 28 type sequence S description binding site for residue CDL b1 404 source : AC4 34) chain b1 residue 29 type sequence S description binding site for residue CDL b1 404 source : AC4 35) chain b1 residue 30 type sequence W description binding site for residue CDL b1 404 source : AC4 36) chain d1 residue 72 type sequence Q description binding site for residue CDL b1 404 source : AC4 37) chain q1 residue 37 type sequence V description binding site for residue CDL b1 404 source : AC4 38) chain q1 residue 40 type sequence R description binding site for residue CDL b1 404 source : AC4 39) chain q1 residue 44 type sequence C description binding site for residue CDL b1 404 source : AC4 40) chain b1 residue 13 type sequence I description binding site for residue CDL b1 405 source : AC5 41) chain b1 residue 198 type sequence L description binding site for residue CDL b1 405 source : AC5 42) chain b2 residue 17 type sequence A description binding site for residue CDL b1 405 source : AC5 43) chain b2 residue 198 type sequence L description binding site for residue CDL b1 405 source : AC5 44) chain b1 residue 142 type sequence G description binding site for residue U10 b1 406 source : AC6 45) chain b1 residue 145 type sequence V description binding site for residue U10 b1 406 source : AC6 46) chain b1 residue 146 type sequence I description binding site for residue U10 b1 406 source : AC6 47) chain b1 residue 149 type sequence L description binding site for residue U10 b1 406 source : AC6 48) chain b1 residue 270 type sequence P description binding site for residue U10 b1 406 source : AC6 49) chain b1 residue 274 type sequence F description binding site for residue U10 b1 406 source : AC6 50) chain b1 residue 278 type sequence Y description binding site for residue U10 b1 406 source : AC6 51) chain b1 residue 281 type sequence L description binding site for residue U10 b1 406 source : AC6 52) chain b1 residue 18 type sequence F description binding site for residue U10 b1 407 source : AC7 53) chain b1 residue 21 type sequence L description binding site for residue U10 b1 407 source : AC7 54) chain b1 residue 31 type sequence W description binding site for residue U10 b1 407 source : AC7 55) chain b1 residue 35 type sequence S description binding site for residue U10 b1 407 source : AC7 56) chain b1 residue 201 type sequence H description binding site for residue U10 b1 407 source : AC7 57) chain b1 residue 220 type sequence F description binding site for residue U10 b1 407 source : AC7 58) chain b1 residue 228 type sequence D description binding site for residue U10 b1 407 source : AC7 59) chain c1 residue 37 type sequence C description binding site for residue HEC c1 501 source : AC8 60) chain c1 residue 39 type sequence S description binding site for residue HEC c1 501 source : AC8 61) chain c1 residue 40 type sequence C description binding site for residue HEC c1 501 source : AC8 62) chain c1 residue 41 type sequence H description binding site for residue HEC c1 501 source : AC8 63) chain c1 residue 108 type sequence A description binding site for residue HEC c1 501 source : AC8 64) chain c1 residue 111 type sequence P description binding site for residue HEC c1 501 source : AC8 65) chain c1 residue 116 type sequence I description binding site for residue HEC c1 501 source : AC8 66) chain c1 residue 120 type sequence R description binding site for residue HEC c1 501 source : AC8 67) chain c1 residue 126 type sequence Y description binding site for residue HEC c1 501 source : AC8 68) chain c1 residue 130 type sequence L description binding site for residue HEC c1 501 source : AC8 69) chain c1 residue 152 type sequence F description binding site for residue HEC c1 501 source : AC8 70) chain c1 residue 158 type sequence G description binding site for residue HEC c1 501 source : AC8 71) chain c1 residue 159 type sequence M description binding site for residue HEC c1 501 source : AC8 72) chain c1 residue 162 type sequence P description binding site for residue HEC c1 501 source : AC8 73) chain b1 residue 75 type sequence Y description binding site for residue 3PE c1 502 source : AC9 74) chain c1 residue 203 type sequence M description binding site for residue 3PE c1 502 source : AC9 75) chain c1 residue 206 type sequence K description binding site for residue 3PE c1 502 source : AC9 76) chain c1 residue 207 type sequence M description binding site for residue 3PE c1 502 source : AC9 77) chain f1 residue 57 type sequence Q description binding site for residue 3PE c1 502 source : AC9 78) chain b1 residue 29 type sequence S description binding site for residue CDL c1 503 source : AD1 79) chain b1 residue 32 type sequence N description binding site for residue CDL c1 503 source : AD1 80) chain b1 residue 231 type sequence G description binding site for residue CDL c1 503 source : AD1 81) chain c1 residue 219 type sequence Y description binding site for residue CDL c1 503 source : AD1 82) chain c1 residue 222 type sequence K description binding site for residue CDL c1 503 source : AD1 83) chain c1 residue 223 type sequence R description binding site for residue CDL c1 503 source : AD1 84) chain c1 residue 230 type sequence K description binding site for residue CDL c1 503 source : AD1 85) chain q1 residue 29 type sequence Y description binding site for residue CDL c1 503 source : AD1 86) chain q1 residue 30 type sequence F description binding site for residue CDL c1 503 source : AD1 87) chain q1 residue 33 type sequence G description binding site for residue CDL c1 503 source : AD1 88) chain q1 residue 37 type sequence V description binding site for residue CDL c1 503 source : AD1 89) chain q1 residue 40 type sequence R description binding site for residue CDL c1 503 source : AD1 90) chain f1 residue 139 type sequence C description binding site for residue FES f1 501 source : AD2 91) chain f1 residue 141 type sequence H description binding site for residue FES f1 501 source : AD2 92) chain f1 residue 142 type sequence L description binding site for residue FES f1 501 source : AD2 93) chain f1 residue 144 type sequence C description binding site for residue FES f1 501 source : AD2 94) chain f1 residue 158 type sequence C description binding site for residue FES f1 501 source : AD2 95) chain f1 residue 161 type sequence H description binding site for residue FES f1 501 source : AD2 96) chain f1 residue 163 type sequence S description binding site for residue FES f1 501 source : AD2 97) chain b2 residue 48 type sequence G description binding site for residue HEM b2 401 source : AD3 98) chain b2 residue 66 type sequence V description binding site for residue HEM b2 401 source : AD3 99) chain b2 residue 80 type sequence R description binding site for residue HEM b2 401 source : AD3 100) chain b2 residue 83 type sequence H description binding site for residue HEM b2 401 source : AD3 101) chain b2 residue 87 type sequence A description binding site for residue HEM b2 401 source : AD3 102) chain b2 residue 90 type sequence F description binding site for residue HEM b2 401 source : AD3 103) chain b2 residue 130 type sequence G description binding site for residue HEM b2 401 source : AD3 104) chain b2 residue 134 type sequence P description binding site for residue HEM b2 401 source : AD3 105) chain b2 residue 182 type sequence H description binding site for residue HEM b2 401 source : AD3 106) chain b2 residue 183 type sequence F description binding site for residue HEM b2 401 source : AD3 107) chain b2 residue 186 type sequence P description binding site for residue HEM b2 401 source : AD3 108) chain b2 residue 31 type sequence W description binding site for residue HEM b2 402 source : AD4 109) chain b2 residue 97 type sequence H description binding site for residue HEM b2 402 source : AD4 110) chain b2 residue 100 type sequence R description binding site for residue HEM b2 402 source : AD4 111) chain b2 residue 106 type sequence S description binding site for residue HEM b2 402 source : AD4 112) chain b2 residue 113 type sequence W description binding site for residue HEM b2 402 source : AD4 113) chain b2 residue 116 type sequence G description binding site for residue HEM b2 402 source : AD4 114) chain b2 residue 117 type sequence V description binding site for residue HEM b2 402 source : AD4 115) chain b2 residue 119 type sequence L description binding site for residue HEM b2 402 source : AD4 116) chain b2 residue 196 type sequence H description binding site for residue HEM b2 402 source : AD4 117) chain b2 residue 200 type sequence L description binding site for residue HEM b2 402 source : AD4 118) chain b2 residue 206 type sequence N description binding site for residue HEM b2 402 source : AD4 119) chain b2 residue 30 type sequence W description binding site for residue 3PE b2 403 source : AD5 120) chain b2 residue 95 type sequence F description binding site for residue 3PE b2 403 source : AD5 121) chain b2 residue 96 type sequence M description binding site for residue 3PE b2 403 source : AD5 122) chain b2 residue 103 type sequence Y description binding site for residue 3PE b2 403 source : AD5 123) chain b2 residue 316 type sequence M description binding site for residue 3PE b2 403 source : AD5 124) chain b2 residue 322 type sequence Q description binding site for residue 3PE b2 403 source : AD5 125) chain b2 residue 326 type sequence W description binding site for residue 3PE b2 403 source : AD5 126) chain b2 residue 332 type sequence L description binding site for residue 3PE b2 403 source : AD5 127) chain b2 residue 358 type sequence Y description binding site for residue 3PE b2 403 source : AD5 128) chain q2 residue 48 type sequence V description binding site for residue 3PE b2 403 source : AD5 129) chain b2 residue 28 type sequence S description binding site for residue CDL b2 404 source : AD6 130) chain b2 residue 29 type sequence S description binding site for residue CDL b2 404 source : AD6 131) chain b2 residue 30 type sequence W description binding site for residue CDL b2 404 source : AD6 132) chain d2 residue 72 type sequence Q description binding site for residue CDL b2 404 source : AD6 133) chain q2 residue 40 type sequence R description binding site for residue CDL b2 404 source : AD6 134) chain q2 residue 41 type sequence T description binding site for residue CDL b2 404 source : AD6 135) chain b2 residue 18 type sequence F description binding site for residue U10 b2 405 source : AD7 136) chain b2 residue 21 type sequence L description binding site for residue U10 b2 405 source : AD7 137) chain b2 residue 31 type sequence W description binding site for residue U10 b2 405 source : AD7 138) chain b2 residue 35 type sequence S description binding site for residue U10 b2 405 source : AD7 139) chain b2 residue 197 type sequence L description binding site for residue U10 b2 405 source : AD7 140) chain b2 residue 201 type sequence H description binding site for residue U10 b2 405 source : AD7 141) chain b2 residue 205 type sequence S description binding site for residue U10 b2 405 source : AD7 142) chain b2 residue 220 type sequence F description binding site for residue U10 b2 405 source : AD7 143) chain b2 residue 29 type sequence S description binding site for residue CDL c2 502 source : AD8 144) chain b2 residue 32 type sequence N description binding site for residue CDL c2 502 source : AD8 145) chain c2 residue 219 type sequence Y description binding site for residue CDL c2 502 source : AD8 146) chain c2 residue 222 type sequence K description binding site for residue CDL c2 502 source : AD8 147) chain c2 residue 223 type sequence R description binding site for residue CDL c2 502 source : AD8 148) chain c2 residue 230 type sequence K description binding site for residue CDL c2 502 source : AD8 149) chain q2 residue 29 type sequence Y description binding site for residue CDL c2 502 source : AD8 150) chain q2 residue 36 type sequence N description binding site for residue CDL c2 502 source : AD8 151) chain q2 residue 37 type sequence V description binding site for residue CDL c2 502 source : AD8 152) chain q2 residue 40 type sequence R description binding site for residue CDL c2 502 source : AD8 153) chain c2 residue 199 type sequence H description binding site for residue 3PE f2 201 source : AD9 154) chain c2 residue 203 type sequence M description binding site for residue 3PE f2 201 source : AD9 155) chain c2 residue 206 type sequence K description binding site for residue 3PE f2 201 source : AD9 156) chain f2 residue 53 type sequence N description binding site for residue 3PE f2 201 source : AD9 157) chain f2 residue 57 type sequence Q description binding site for residue 3PE f2 201 source : AD9 158) chain i2 residue 36 type sequence D description binding site for residue 3PE f2 201 source : AD9 159) chain f2 residue 139 type sequence C description binding site for residue FES f2 202 source : AE1 160) chain f2 residue 141 type sequence H description binding site for residue FES f2 202 source : AE1 161) chain f2 residue 142 type sequence L description binding site for residue FES f2 202 source : AE1 162) chain f2 residue 158 type sequence C description binding site for residue FES f2 202 source : AE1 163) chain f2 residue 161 type sequence H description binding site for residue FES f2 202 source : AE1 164) chain f2 residue 163 type sequence S description binding site for residue FES f2 202 source : AE1 165) chain c2 residue 36 type sequence V description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 166) chain c2 residue 37 type sequence C description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 167) chain c2 residue 39 type sequence S description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 168) chain c2 residue 41 type sequence H description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 169) chain c2 residue 105 type sequence N description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 170) chain c2 residue 108 type sequence A description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 171) chain c2 residue 110 type sequence P description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 172) chain c2 residue 116 type sequence I description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 173) chain c2 residue 120 type sequence R description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 174) chain c2 residue 126 type sequence Y description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 175) chain c2 residue 130 type sequence L description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 176) chain c2 residue 152 type sequence F description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 177) chain c2 residue 158 type sequence G description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 178) chain c2 residue 159 type sequence M description binding site for Di-peptide HEC c2 501 and CYS c2 40 source : AE2 179) chain c2 residue 33 type sequence Y description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 180) chain c2 residue 36 type sequence V description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 181) chain c2 residue 38 type sequence S description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 182) chain c2 residue 39 type sequence S description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 183) chain c2 residue 40 type sequence C description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 184) chain c2 residue 41 type sequence H description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 185) chain c2 residue 105 type sequence N description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 186) chain c2 residue 108 type sequence A description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 187) chain c2 residue 110 type sequence P description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 188) chain c2 residue 116 type sequence I description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 189) chain c2 residue 120 type sequence R description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 190) chain c2 residue 126 type sequence Y description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 191) chain c2 residue 130 type sequence L description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 192) chain c2 residue 152 type sequence F description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 193) chain c2 residue 158 type sequence G description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 194) chain c2 residue 159 type sequence M description binding site for Di-peptide HEC c2 501 and CYS c2 37 source : AE3 195) chain b1 residue 83 type BINDING sequence H description axial binding residue => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI2 196) chain b1 residue 97 type BINDING sequence H description axial binding residue => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI2 197) chain b1 residue 182 type BINDING sequence H description axial binding residue => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI2 198) chain b1 residue 196 type BINDING sequence H description axial binding residue => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI2 199) chain b2 residue 83 type BINDING sequence H description axial binding residue => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI2 200) chain b2 residue 97 type BINDING sequence H description axial binding residue => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI2 201) chain b2 residue 182 type BINDING sequence H description axial binding residue => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI2 202) chain b2 residue 196 type BINDING sequence H description axial binding residue => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI2 203) chain b1 residue 201 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI3 204) chain b2 residue 201 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI3 205) chain b1 residue 33-53 type TRANSMEM sequence FGSLLGICLILQILTGLFLAM description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 206) chain b2 residue 77-98 type TRANSMEM sequence WIIRYMHANGASMFFICLFMHV description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 207) chain b2 residue 113-133 type TRANSMEM sequence WNIGVILLFATMATAFMGYVL description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 208) chain b2 residue 178-198 type TRANSMEM sequence FFAFHFIFPFIIAALAMVHLL description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 209) chain b2 residue 226-246 type TRANSMEM sequence IKDILGAILLILILMLLVLFT description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 210) chain b2 residue 288-308 type TRANSMEM sequence LGGVLALVLSILVLVIMPLLH description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 211) chain b2 residue 320-340 type TRANSMEM sequence ISQCMFWILVADLLTLTWIGG description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 212) chain b2 residue 347-367 type TRANSMEM sequence YIIIGQLASIMYFLIILVMMP description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 213) chain b1 residue 77-98 type TRANSMEM sequence WIIRYMHANGASMFFICLFMHV description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 214) chain b1 residue 113-133 type TRANSMEM sequence WNIGVILLFATMATAFMGYVL description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 215) chain b1 residue 178-198 type TRANSMEM sequence FFAFHFIFPFIIAALAMVHLL description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 216) chain b1 residue 226-246 type TRANSMEM sequence IKDILGAILLILILMLLVLFT description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 217) chain b1 residue 288-308 type TRANSMEM sequence LGGVLALVLSILVLVIMPLLH description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 218) chain b1 residue 320-340 type TRANSMEM sequence ISQCMFWILVADLLTLTWIGG description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 219) chain b1 residue 347-367 type TRANSMEM sequence YIIIGQLASIMYFLIILVMMP description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 220) chain b2 residue 33-53 type TRANSMEM sequence FGSLLGICLILQILTGLFLAM description Helical => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI1 221) chain a2 residue 54-77 type prosite sequence GSRYENFNNLGTSHLLRLASSLTT description INSULINASE Insulinase family, zinc-binding region signature. GsryenfnnlGtSHLLRLAsSlTT source prosite : PS00143

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