eF-site ID 3aec-ABCD PDB Code 3aec Chain A, B, C, D click to enlarge Title Crystal structure of porcine heart mitochondrial complex II bound with 2-Iodo-N-(1-methylethyl)-benzamid Classification OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR Compound Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial Source ORGANISM_COMMON: Pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence A:  STQYPVVDHEFDAVVVGAGGAGLRAAFGLSEAGFNTACVT KLFPTRSHTVAAQGGINAALGNMEEDNWRWHFYDTVKGSD WLGDQDAIHYMTEQAPASVVELENYGMPFSRTEDGKIYQR AFGGQSLKFGKGGQAHRCCCVADRTGHSLLHTLYGRSLRY DTSYFVEYFALDLLMENGECRGVIALCIEDGSIHRIRARN TVVATGGYGRTYFSCTSAHTSTGDGTAMVTRAGLPCQDLE FVQFHPTGIYGAGCLITEGCRGEGGILINSQGERFMERYA PVAKDLASRDVVSRSMTLEIREGRGCGPEKDHVYLQLHHL PPEQLAVRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMG GIPTNYKGQVLRHVNGQDQVVPGLYACGEAACASVHGANR LGANSLLDLVVFGRACALSIAESCRPGDKVPSIKPNAGEE SVMNLDKLRFANGTIRTSELRLSMQKSMQSHAAVFRVGSV LQEGCEKILRLYGDLQHLKTFDRGMVWNTDLVETLELQNL MLCALQTIYGAEARKESRGAHAREDFKERVDEYDYSKPIQ GQQKKPFQEHWRKHTLSYVDVKTGKVSLEYRPVIDKTLNE ADCATVPPAIRSY B:  PRIKKFAIYRWDPDKTGDKPHMQTYEIDLNNCGPMVLDAL IKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRR IDTNLDKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPY LKKKDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSC PSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQD PFSLYRCHTIMNCTGTCPKGLNPGKAIAEIKKMMATYKE C:  TTAKEEMERFWNKNLGSNRPLSPHITIYRWSLPMAMSICH RGTGIALSAGVSLFGLSALLLPGNFESHLELVKSLCLGPT LIYTAKFGIVFPLMYHTWNGIRHLIWDLGKGLTIPQLTQS GVVVLILTVLSSVGLAAM D:  SSKAASLHWTGERVVSVLLLGLLPAAYLNPCSAMDYSLAA ALTLHGHWGIGQVVTDYVRGDALQKAAKAGLLALSAFTFA GLCYFNYHDVGICKAVAMLWKL Description Functional site 1) chain A residue 26 type sequence G description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 2) chain A residue 27 type sequence A description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 3) chain A residue 28 type sequence G description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 4) chain A residue 29 type sequence G description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 5) chain A residue 30 type sequence A description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 6) chain A residue 49 type sequence T description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 7) chain A residue 50 type sequence K description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 8) chain A residue 51 type sequence L description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 9) chain A residue 56 type sequence S description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 10) chain A residue 57 type sequence H description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 11) chain A residue 58 type sequence T description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 12) chain A residue 60 type sequence A description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 13) chain A residue 61 type sequence A description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 14) chain A residue 62 type sequence Q description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 15) chain A residue 63 type sequence G description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 16) chain A residue 64 type sequence G description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 17) chain A residue 177 type sequence Y description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 18) chain A residue 178 type sequence F description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 19) chain A residue 179 type sequence A description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 20) chain A residue 214 type sequence T description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 21) chain A residue 215 type sequence G description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 22) chain A residue 225 type sequence T description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 23) chain A residue 226 type sequence S description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 24) chain A residue 233 type sequence D description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 25) chain A residue 398 type sequence E description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 26) chain A residue 409 type sequence R description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 27) chain A residue 412 type sequence A description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 28) chain A residue 414 type sequence S description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 29) chain A residue 415 type sequence L description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 30) chain A residue 418 type sequence L description BINDING SITE FOR RESIDUE FAD A 700 source : AC1 31) chain B residue 64 type sequence S description BINDING SITE FOR RESIDUE FES B 302 source : AC2 32) chain B residue 65 type sequence C description BINDING SITE FOR RESIDUE FES B 302 source : AC2 33) chain B residue 66 type sequence R description BINDING SITE FOR RESIDUE FES B 302 source : AC2 34) chain B residue 68 type sequence G description BINDING SITE FOR RESIDUE FES B 302 source : AC2 35) chain B residue 70 type sequence C description BINDING SITE FOR RESIDUE FES B 302 source : AC2 36) chain B residue 71 type sequence G description BINDING SITE FOR RESIDUE FES B 302 source : AC2 37) chain B residue 73 type sequence C description BINDING SITE FOR RESIDUE FES B 302 source : AC2 38) chain B residue 85 type sequence C description BINDING SITE FOR RESIDUE FES B 302 source : AC2 39) chain B residue 158 type sequence C description BINDING SITE FOR RESIDUE SF4 B 303 source : AC3 40) chain B residue 159 type sequence I description BINDING SITE FOR RESIDUE SF4 B 303 source : AC3 41) chain B residue 161 type sequence C description BINDING SITE FOR RESIDUE SF4 B 303 source : AC3 42) chain B residue 162 type sequence A description BINDING SITE FOR RESIDUE SF4 B 303 source : AC3 43) chain B residue 164 type sequence C description BINDING SITE FOR RESIDUE SF4 B 303 source : AC3 44) chain B residue 182 type sequence A description BINDING SITE FOR RESIDUE SF4 B 303 source : AC3 45) chain B residue 225 type sequence C description BINDING SITE FOR RESIDUE SF4 B 303 source : AC3 46) chain B residue 226 type sequence P description BINDING SITE FOR RESIDUE SF4 B 303 source : AC3 47) chain B residue 168 type sequence C description BINDING SITE FOR RESIDUE F3S B 304 source : AC4 48) chain B residue 178 type sequence Y description BINDING SITE FOR RESIDUE F3S B 304 source : AC4 49) chain B residue 181 type sequence P description BINDING SITE FOR RESIDUE F3S B 304 source : AC4 50) chain B residue 215 type sequence C description BINDING SITE FOR RESIDUE F3S B 304 source : AC4 51) chain B residue 216 type sequence H description BINDING SITE FOR RESIDUE F3S B 304 source : AC4 52) chain B residue 217 type sequence T description BINDING SITE FOR RESIDUE F3S B 304 source : AC4 53) chain B residue 218 type sequence I description BINDING SITE FOR RESIDUE F3S B 304 source : AC4 54) chain B residue 219 type sequence M description BINDING SITE FOR RESIDUE F3S B 304 source : AC4 55) chain B residue 220 type sequence N description BINDING SITE FOR RESIDUE F3S B 304 source : AC4 56) chain B residue 221 type sequence C description BINDING SITE FOR RESIDUE F3S B 304 source : AC4 57) chain B residue 216 type sequence H description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 58) chain C residue 45 type sequence H description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 59) chain C residue 46 type sequence R description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 60) chain C residue 49 type sequence G description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 61) chain C residue 52 type sequence L description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 62) chain C residue 53 type sequence S description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 63) chain C residue 101 type sequence H description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 64) chain C residue 108 type sequence H description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 65) chain D residue 53 type sequence L description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 66) chain D residue 57 type sequence L description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 67) chain D residue 79 type sequence H description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 68) chain D residue 83 type sequence G description BINDING SITE FOR RESIDUE HEM C 1305 source : AC5 69) chain C residue 140 type sequence L description BINDING SITE FOR RESIDUE EPH D 1306 source : AC6 70) chain D residue 60 type sequence A description BINDING SITE FOR RESIDUE EPH D 1306 source : AC6 71) chain D residue 61 type sequence Y description BINDING SITE FOR RESIDUE EPH D 1306 source : AC6 72) chain D residue 62 type sequence L description BINDING SITE FOR RESIDUE EPH D 1306 source : AC6 73) chain D residue 64 type sequence P description BINDING SITE FOR RESIDUE EPH D 1306 source : AC6 74) chain D residue 127 type sequence C description BINDING SITE FOR RESIDUE EPH D 1306 source : AC6 75) chain D residue 131 type sequence A description BINDING SITE FOR RESIDUE EPH D 1306 source : AC6 76) chain D residue 134 type sequence W description BINDING SITE FOR RESIDUE EPH D 1306 source : AC6 77) chain B residue 170 type sequence S description BINDING SITE FOR RESIDUE EBM C 1201 source : AC7 78) chain B residue 173 type sequence W description BINDING SITE FOR RESIDUE EBM C 1201 source : AC7 79) chain B residue 216 type sequence H description BINDING SITE FOR RESIDUE EBM C 1201 source : AC7 80) chain B residue 218 type sequence I description BINDING SITE FOR RESIDUE EBM C 1201 source : AC7 81) chain C residue 42 type sequence S description BINDING SITE FOR RESIDUE EBM C 1201 source : AC7 82) chain C residue 46 type sequence R description BINDING SITE FOR RESIDUE EBM C 1201 source : AC7 83) chain D residue 90 type sequence D description BINDING SITE FOR RESIDUE EBM C 1201 source : AC7 84) chain D residue 91 type sequence Y description BINDING SITE FOR RESIDUE EBM C 1201 source : AC7 85) chain B residue 65-73 type prosite sequence CREGICGSC description 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CREGICGSC source prosite : PS00197 86) chain B residue 158-169 type prosite sequence CILCACCSTSCP description 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCStSCP source prosite : PS00198 87) chain A residue 55-64 type prosite sequence RSHTVAAQGG description FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAqGG source prosite : PS00504 88) chain C residue 24-48 type prosite sequence RPLSPHITIYRWSLPMAMSICHRGT description SDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPLsphItiyrwsLpmamSicHRgT source prosite : PS01000 89) chain C residue 101-114 type prosite sequence HTWNGIRHLIWDLG description SDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HtwnGIRHLiWDlG source prosite : PS01001 90) chain D residue 41-62 type TRANSMEM sequence LHWTGERVVSVLLLGLLPAAYL description Helical => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI1 91) chain B residue 221 type TRANSMEM sequence C description Helical => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI1 92) chain B residue 225 type TRANSMEM sequence C description Helical => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI1 93) chain D residue 68-88 type TRANSMEM sequence MDYSLAAALTLHGHWGIGQVV description Helical => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI1 94) chain D residue 98-119 type TRANSMEM sequence QKAAKAGLLALSAFTFAGLCYF description Helical => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI1 95) chain B residue 85 type TRANSMEM sequence C description Helical => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI1 96) chain B residue 158 type TRANSMEM sequence C description Helical => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI1 97) chain B residue 161 type TRANSMEM sequence C description Helical => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI1 98) chain B residue 164 type TRANSMEM sequence C description Helical => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI1 99) chain B residue 168 type TRANSMEM sequence C description Helical => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI1 100) chain B residue 215 type TRANSMEM sequence C description Helical => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI1 101) chain D residue 63-67 type TOPO_DOM sequence NPCSA description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 102) chain A residue 254 type TOPO_DOM sequence H description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 103) chain A residue 266 type TOPO_DOM sequence T description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 104) chain A residue 365 type TOPO_DOM sequence H description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 105) chain A residue 398 type TOPO_DOM sequence E description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 106) chain A residue 409 type TOPO_DOM sequence R description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 107) chain A residue 412 type TOPO_DOM sequence A description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 108) chain A residue 414 type TOPO_DOM sequence S description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 109) chain A residue 415 type TOPO_DOM sequence L description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 110) chain D residue 120-136 type TOPO_DOM sequence NYHDVGICKAVAMLWKL description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 111) chain C residue 119-140 type TOPO_DOM sequence IPQLTQSGVVVLILTVLSSVGL description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 112) chain A residue 50 type TOPO_DOM sequence K description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 113) chain A residue 56 type TOPO_DOM sequence S description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 114) chain A residue 58 type TOPO_DOM sequence T description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 115) chain A residue 63 type TOPO_DOM sequence G description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 116) chain A residue 179 type TOPO_DOM sequence A description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 117) chain A residue 233 type TOPO_DOM sequence D description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI2 118) chain D residue 89-97 type TOPO_DOM sequence TDYVRGDAL description Mitochondrial matrix => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI3 119) chain C residue 141-143 type TOPO_DOM sequence AAM description Mitochondrial matrix => ECO:0000305|PubMed:15989954 source Swiss-Prot : SWS_FT_FI3 120) chain D residue 79 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0 source Swiss-Prot : SWS_FT_FI4 121) chain A residue 605 type BINDING sequence K description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0 source Swiss-Prot : SWS_FT_FI4 122) chain A residue 140 type BINDING sequence K description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0 source Swiss-Prot : SWS_FT_FI4 123) chain A residue 438 type BINDING sequence K description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0 source Swiss-Prot : SWS_FT_FI4 124) chain A residue 475 type BINDING sequence K description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0 source Swiss-Prot : SWS_FT_FI4 125) chain A residue 508 type BINDING sequence K description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0 source Swiss-Prot : SWS_FT_FI4 126) chain A residue 556 type BINDING sequence K description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0 source Swiss-Prot : SWS_FT_FI4 127) chain A residue 582 type BINDING sequence K description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0 source Swiss-Prot : SWS_FT_FI4 128) chain A residue 591 type BINDING sequence K description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0 source Swiss-Prot : SWS_FT_FI4 129) chain A residue 594 type BINDING sequence K description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0 source Swiss-Prot : SWS_FT_FI4 130) chain D residue 91 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15989954 source Swiss-Prot : SWS_FT_FI5 131) chain A residue 293 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15989954 source Swiss-Prot : SWS_FT_FI5 132) chain A residue 443 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15989954 source Swiss-Prot : SWS_FT_FI5 133) chain A residue 456 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15989954 source Swiss-Prot : SWS_FT_FI5 134) chain A residue 496 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15989954 source Swiss-Prot : SWS_FT_FI5 135) chain A residue 173 type MOD_RES sequence Y description Phosphotyrosine; by SRC => ECO:0000250|UniProtKB:P31040 source Swiss-Prot : SWS_FT_FI6 136) chain A residue 566 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P31040 source Swiss-Prot : SWS_FT_FI7 137) chain A residue 573 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q8K2B3 source Swiss-Prot : SWS_FT_FI8

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