eF-site ID 3bcc-ABCDEFGHIJ PDB Code 3bcc Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN Classification OXIDOREDUCTASE Compound UBIQUINOL CYTOCHROME C OXIDOREDUCTASE Source ORGANISM_COMMON: chicken; ORGANISM_SCIENTIFIC: Gallus gallus; Sequence A:  YAQALQSVPETQVSQLDNGVRVASEQSSQPTCTVGVWIDA GSRYESEKNNGAGYFLEHLAFKGTKNRPQNALEKEVESMG AHLNAYSSREHTAYYIKALSKDVPKAVELLADIVQNCSLE DSQIEKERDVIVRELQENDTSMREVVFNYLHATAFQGTGL AQSVEGPSENIRKLSRADLTEYLSTHYTAPRMVLAAAGGV EHQQLLELAQKHFGGVPFTYDDDAVPTLSKCRFTGSQIRH REDGLPLAHVAIAVEGPGWAHPDLVALQVANAIIGHYDRT YGGGLHSSSPLASIAVTNKLCQSFQTFSICYSETGLFGFY FVCDRMSIDDMMFVLQGQWMRLCTSISESEVLRGKNFLRN ALVSHLDGTTPVCEDIGRELLTYGRRIPLEEWEERLAEVD ARMVREVCSKYIYDQCPAVAGPGPIEQLPDYNRIRSGMFW LR B:  PPHPQDLEITKLPNGLVIASLENYSPGSTIGVFIKAGSRY ENSSNLGTSHLLRLASSLTTKGASSFKITRGIEAVGGKLS VESTRENMAYTVECLRDDVEILMEFLLNVTTAPEFRPWEV ADLQPQLKIDKAVAFQNPQTHVIENLHAAAYRNALADSLY CPDYRIGKVTSVELHDFVQNHFTSARMALVGLGVSHPVLK NVAEQLLNIRGGLGLSGAKAKYRGGEIREQNGDSLVHAAI VAESAAIGGAEANAFSVLQHVLGANPHVKRGNPFDVSAFN ASYSDSGLFGFYTISQAAYAGQVIKAAYNQVKTIAQGNVS NENVQAAKNKLKAKYLMSVESSEGFLEEVGSQALAAGSYN PPSTVLQQIDAVADADVIKAAKKFVSRQKSMAASGNLGHT PFVDEL C:  APNIRKSHPLLKMINNSLIDLPAPSNISAWWNFGSLLAVC LMTQILTGLLLAMHYTADTSLAFSSVAHTCRNVQYGWLIR NLHANGASFFFICIFLHIGRGLYYGSYLYKETWNTGVILL LTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGHTL VEWAWGGFSVDNPTLTRFFALHFLLPFAIAGITIIHLTFL HESGSNNPLGISSDSDKIPFHPYYSFKDILGLTLMLTPFL TLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAI LRSIPNKLGGVLALAASVLILFLIPFLHKSKQRTMTFRPL SQTLFWLLVANLLILTWIGSQPVEHPFIIIGQMASLSYFT ILLILFPTIGTLENKMLNY D:  SDLELHPPSYPWSHRGPLSSLDHTSIRRGFQVYKQVCSSC HSMDYVAYRHLVGVCYTEDEAKALAEEVEVQDGPNEDGEM FMRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRAR HGGEDYVFSLLTGYCEPPTGVSVREGLYFNPYFPGQAIGM APPIYNDVLEFDDGTPATMSQVAKDVCTFLRWAAEPEHDH RKRMGLKMLLMMGLLVPLVYYMKRHKWSVLKSRKLAYRPP K E:  SHTDIKVPNFSDYRRPPDDYSTKSSRESDPSRKGFSYLVT AVTTLGVAYAAKNVVTQFVSSMSASADVLAMSKIEIKLSD IPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDP QHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPC HGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG F:  SRWLEGIRKWYYNAAGFNKYGLMRDDTIYENDDVKEAIRR LPENLYDDRMFRIKRALDLNMRQQILPKEQWTKYEEDVPY LEPYLKEVIRERKEREEWDK G:  RQFGHLTRVRHLITYSLSPFEQRPFPHYFSKGVPNVWRRL RACILRVAPPFLAFYLLYTWGTQEFEKSKRKNPAAYVN H:  LVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSQTEE DCTEELFDFLHARDHCVAHKLFNSLK I:  XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX J:  TLTARLYSLLFRRTSTFALTIVVGALLFERAFDQGADAIY EHINEGKLWKHIKHKYENK Description Functional site 1) chain C residue 45 type sequence Q description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 2) chain C residue 46 type sequence I description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 3) chain C residue 49 type sequence G description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 4) chain C residue 50 type sequence L description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 5) chain C residue 52 type sequence L description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 6) chain C residue 53 type sequence A description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 7) chain C residue 81 type sequence R description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 8) chain C residue 84 type sequence H description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 9) chain C residue 85 type sequence A description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 10) chain C residue 124 type sequence L description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 11) chain C residue 127 type sequence T description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 12) chain C residue 128 type sequence A description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 13) chain C residue 131 type sequence G description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 14) chain C residue 132 type sequence Y description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 15) chain C residue 134 type sequence L description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 16) chain C residue 135 type sequence P description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 17) chain C residue 183 type sequence H description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 18) chain C residue 184 type sequence F description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 19) chain C residue 187 type sequence P description BINDING SITE FOR RESIDUE HEM C 381 source : AC1 20) chain C residue 32 type sequence W description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 21) chain C residue 34 type sequence F description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 22) chain C residue 35 type sequence G description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 23) chain C residue 36 type sequence S description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 24) chain C residue 38 type sequence L description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 25) chain C residue 39 type sequence A description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 26) chain C residue 98 type sequence H description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 27) chain C residue 99 type sequence I description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 28) chain C residue 101 type sequence R description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 29) chain C residue 107 type sequence S description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 30) chain C residue 110 type sequence Y description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 31) chain C residue 114 type sequence W description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 32) chain C residue 117 type sequence G description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 33) chain C residue 118 type sequence V description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 34) chain C residue 120 type sequence L description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 35) chain C residue 121 type sequence L description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 36) chain C residue 194 type sequence T description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 37) chain C residue 197 type sequence H description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 38) chain C residue 201 type sequence L description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 39) chain C residue 207 type sequence N description BINDING SITE FOR RESIDUE HEM C 382 source : AC2 40) chain D residue 36 type sequence V description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 41) chain D residue 37 type sequence C description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 42) chain D residue 40 type sequence C description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 43) chain D residue 41 type sequence H description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 44) chain D residue 105 type sequence N description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 45) chain D residue 110 type sequence P description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 46) chain D residue 111 type sequence P description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 47) chain D residue 120 type sequence R description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 48) chain D residue 126 type sequence Y description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 49) chain D residue 153 type sequence F description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 50) chain D residue 158 type sequence I description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 51) chain D residue 159 type sequence G description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 52) chain D residue 160 type sequence M description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 53) chain D residue 163 type sequence P description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 54) chain D residue 186 type sequence V description BINDING SITE FOR RESIDUE HEM D 242 source : AC3 55) chain E residue 139 type sequence C description BINDING SITE FOR RESIDUE FES E 197 source : AC4 56) chain E residue 141 type sequence H description BINDING SITE FOR RESIDUE FES E 197 source : AC4 57) chain E residue 144 type sequence C description BINDING SITE FOR RESIDUE FES E 197 source : AC4 58) chain E residue 158 type sequence C description BINDING SITE FOR RESIDUE FES E 197 source : AC4 59) chain E residue 160 type sequence C description BINDING SITE FOR RESIDUE FES E 197 source : AC4 60) chain E residue 161 type sequence H description BINDING SITE FOR RESIDUE FES E 197 source : AC4 61) chain E residue 162 type sequence G description BINDING SITE FOR RESIDUE FES E 197 source : AC4 62) chain E residue 163 type sequence S description BINDING SITE FOR RESIDUE FES E 197 source : AC4 63) chain C residue 125 type sequence M description BINDING SITE FOR RESIDUE SIG C 383 source : AC5 64) chain C residue 129 type sequence F description BINDING SITE FOR RESIDUE SIG C 383 source : AC5 65) chain C residue 130 type sequence V description BINDING SITE FOR RESIDUE SIG C 383 source : AC5 66) chain C residue 146 type sequence V description BINDING SITE FOR RESIDUE SIG C 383 source : AC5 67) chain C residue 147 type sequence I description BINDING SITE FOR RESIDUE SIG C 383 source : AC5 68) chain C residue 182 type sequence L description BINDING SITE FOR RESIDUE SIG C 383 source : AC5 69) chain C residue 271 type sequence P description BINDING SITE FOR RESIDUE SIG C 383 source : AC5 70) chain C residue 275 type sequence F description BINDING SITE FOR RESIDUE SIG C 383 source : AC5 71) chain C residue 279 type sequence Y description BINDING SITE FOR RESIDUE SIG C 383 source : AC5 72) chain C residue 295 type sequence L description BINDING SITE FOR RESIDUE SIG C 383 source : AC5 73) chain C residue 18 type sequence S description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 74) chain C residue 32 type sequence W description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 75) chain C residue 33 type sequence N description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 76) chain C residue 35 type sequence G description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 77) chain C residue 36 type sequence S description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 78) chain C residue 39 type sequence A description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 79) chain C residue 42 type sequence L description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 80) chain C residue 43 type sequence M description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 81) chain C residue 191 type sequence A description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 82) chain C residue 194 type sequence T description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 83) chain C residue 195 type sequence I description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 84) chain C residue 198 type sequence L description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 85) chain C residue 221 type sequence F description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 86) chain C residue 225 type sequence Y description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 87) chain C residue 228 type sequence K description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 88) chain C residue 229 type sequence D description BINDING SITE FOR RESIDUE AMY C 384 source : AC6 89) chain B residue 54-77 type prosite sequence GSRYENSSNLGTSHLLRLASSLTT description INSULINASE Insulinase family, zinc-binding region signature. GsryenssnlGtSHLLRLAsSlTT source prosite : PS00143 90) chain D residue 124 type TOPO_DOM sequence E description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 91) chain C residue 114-134 type TOPO_DOM sequence WNTGVILLLTLMATAFVGYVL description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 92) chain C residue 179-199 type TOPO_DOM sequence FFALHFLLPFAIAGITIIHLT description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 93) chain C residue 227-247 type TOPO_DOM sequence FKDILGLTLMLTPFLTLALFS description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 94) chain C residue 289-309 type TOPO_DOM sequence LGGVLALAASVLILFLIPFLH description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 95) chain C residue 321-341 type TOPO_DOM sequence LSQTLFWLLVANLLILTWIGS description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 96) chain C residue 348-368 type TOPO_DOM sequence FIIIGQMASLSYFTILLILFP description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 97) chain J residue 22-47 type TRANSMEM sequence LTIVVGALLFERAFDQGADAIYEHIN description Helical => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI2 98) chain F residue 83 type TRANSMEM sequence Y description Helical => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI2 99) chain F residue 96 type TRANSMEM sequence E description Helical => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI2 100) chain G residue 33 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CQ69 source Swiss-Prot : SWS_FT_FI3 101) chain F residue 88 type MOD_RES sequence P description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CQ69 source Swiss-Prot : SWS_FT_FI3 102) chain E residue 139 type BINDING sequence C description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY source Swiss-Prot : SWS_FT_FI4 103) chain E residue 141 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY source Swiss-Prot : SWS_FT_FI4 104) chain E residue 158 type BINDING sequence C description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY source Swiss-Prot : SWS_FT_FI4 105) chain E residue 161 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY source Swiss-Prot : SWS_FT_FI4 106) chain E residue 163 type BINDING sequence S description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY source Swiss-Prot : SWS_FT_FI4 107) chain C residue 202 type BINDING sequence H description BINDING => ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928, ECO:0000269|PubMed:9565029, ECO:0007744|PDB:1BCC, ECO:0007744|PDB:3CWB, ECO:0007744|PDB:3H1K, ECO:0007744|PDB:3L72 source Swiss-Prot : SWS_FT_FI5

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