eF-site ID 6gci-AB PDB Code 6gci Chain A, B click to enlarge Title Structure of the bongkrekic acid-inhibited mitochondrial ADP/ATP carrier Classification MEMBRANE PROTEIN Compound mitochondrial ADP/ATP carrier Source (6GCI) Sequence A:  GMPPFVVDFLMGGVSAAVSKTAAAPIERIKLLVQNQDEMI KAGRLDRRYNGIIDCFRRTTADEGLMALWRGNTANVIRYF PTQALNFAFRDKFKAMFGYKKDKDGYAKWMAGNLASGGAA GATSLLFVYSLDYARTRLANDAKSAKGGGARQFNGLIDVY RKTLASDGIAGLYRGFGPSVAGIVVYRGLYFGMYDSIKPV VLVGPLANNFLASFLLGWCVTTGAGIASYPLDTVRRRMMM TSKYKSSIDAFRQIIAKEGVKSLFKGAGANILRGVAGAGV LSIYDQLKILLF B:  QVQLVESGGGLVQAGDSLRLACAASGITFSSYTMGWFRQA PGKEREYIARITGSGSNTYYADSVKGRYTISRDNAKNTAY LQMNSLKPEDTANYYCAARDDGRMYQGFYDFEYWGQGTQV TVSS Description Functional site 1) chain A residue 30 type sequence K description binding site for residue BKC A 401 source : AC1 2) chain A residue 88 type sequence R description binding site for residue BKC A 401 source : AC1 3) chain A residue 89 type sequence Y description binding site for residue BKC A 401 source : AC1 4) chain A residue 92 type sequence T description binding site for residue BKC A 401 source : AC1 5) chain A residue 93 type sequence Q description binding site for residue BKC A 401 source : AC1 6) chain A residue 96 type sequence N description binding site for residue BKC A 401 source : AC1 7) chain A residue 135 type sequence L description binding site for residue BKC A 401 source : AC1 8) chain A residue 193 type sequence I description binding site for residue BKC A 401 source : AC1 9) chain A residue 196 type sequence Y description binding site for residue BKC A 401 source : AC1 10) chain A residue 197 type sequence R description binding site for residue BKC A 401 source : AC1 11) chain A residue 200 type sequence Y description binding site for residue BKC A 401 source : AC1 12) chain A residue 287 type sequence R description binding site for residue BKC A 401 source : AC1 13) chain A residue 291 type sequence G description binding site for residue BKC A 401 source : AC1 14) chain A residue 136 type sequence L description binding site for residue CDL A 802 source : AC2 15) chain A residue 183 type sequence Y description binding site for residue CDL A 802 source : AC2 16) chain A residue 184 type sequence R description binding site for residue CDL A 802 source : AC2 17) chain A residue 185 type sequence G description binding site for residue CDL A 802 source : AC2 18) chain A residue 186 type sequence F description binding site for residue CDL A 802 source : AC2 19) chain A residue 187 type sequence G description binding site for residue CDL A 802 source : AC2 20) chain A residue 188 type sequence P description binding site for residue CDL A 802 source : AC2 21) chain A residue 228 type sequence W description binding site for residue CDL A 802 source : AC2 22) chain A residue 260 type sequence S description binding site for residue CDL A 802 source : AC2 23) chain A residue 261 type sequence S description binding site for residue CDL A 802 source : AC2 24) chain A residue 79 type sequence W description binding site for residue CDL A 800 source : AC3 25) chain A residue 81 type sequence G description binding site for residue CDL A 800 source : AC3 26) chain A residue 82 type sequence N description binding site for residue CDL A 800 source : AC3 27) chain A residue 83 type sequence T description binding site for residue CDL A 800 source : AC3 28) chain A residue 278 type sequence F description binding site for residue CDL A 801 source : AC4 29) chain A residue 279 type sequence K description binding site for residue CDL A 801 source : AC4 30) chain A residue 280 type sequence G description binding site for residue CDL A 801 source : AC4 31) chain A residue 281 type sequence A description binding site for residue CDL A 801 source : AC4 32) chain A residue 282 type sequence G description binding site for residue CDL A 801 source : AC4 33) chain A residue 283 type sequence A description binding site for residue CDL A 801 source : AC4 34) chain A residue 165 type sequence G description binding site for residue CDL A 803 source : AC5 35) chain A residue 166 type sequence L description binding site for residue CDL A 803 source : AC5 36) chain A residue 167 type sequence I description binding site for residue CDL A 803 source : AC5 37) chain A residue 61 type sequence G description binding site for residue CDL A 804 source : AC6 38) chain A residue 62 type sequence I description binding site for residue CDL A 804 source : AC6 39) chain A residue 63 type sequence I description binding site for residue CDL A 804 source : AC6 40) chain B residue 45 type sequence R description binding site for residue P6G B 301 source : AC7 41) chain B residue 45 type sequence R description binding site for residue P6G B 301 source : AC7 42) chain B residue 93 type sequence N description binding site for residue P6G B 301 source : AC7 43) chain B residue 93 type sequence N description binding site for residue P6G B 301 source : AC7 44) chain B residue 109 type sequence Y description binding site for residue P6G B 301 source : AC7 45) chain B residue 109 type sequence Y description binding site for residue P6G B 301 source : AC7 46) chain B residue 114 type sequence W description binding site for residue P6G B 301 source : AC7 47) chain B residue 114 type sequence W description binding site for residue P6G B 301 source : AC7 48) chain B residue 116 type sequence Q description binding site for residue P6G B 301 source : AC7 49) chain B residue 116 type sequence Q description binding site for residue P6G B 301 source : AC7 50) chain A residue 30 type BINDING sequence K description BINDING => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI9 51) chain A residue 62 type BINDING sequence I description BINDING => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI9 52) chain A residue 81 type BINDING sequence G description BINDING => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI9 53) chain A residue 96 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI9 54) chain A residue 166 type BINDING sequence L description BINDING => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI9 55) chain A residue 184 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI9 56) chain A residue 196 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI9 57) chain A residue 260 type BINDING sequence S description BINDING => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI9 58) chain A residue 280 type BINDING sequence G description BINDING => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI9 59) chain A residue 88 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P18238 source Swiss-Prot : SWS_FT_FI10 60) chain A residue 245 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P18238 source Swiss-Prot : SWS_FT_FI10 61) chain A residue 105-115 type TOPO_DOM sequence AMFGYKKDKDG description Mitochondrial intermembrane => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 62) chain A residue 214-216 type TOPO_DOM sequence GPL description Mitochondrial intermembrane => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 63) chain A residue 14-37 type TRANSMEM sequence PFVVDFLMGGVSAAVSKTAAAPIE description Helical; Name=1 => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI2 64) chain A residue 38-80 type TOPO_DOM sequence RIKLLVQNQDEMIKAGRLDRRYNGIIDCFRRTTADEGLMA LWR description Mitochondrial matrix => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 65) chain A residue 146-184 type TOPO_DOM sequence TRLANDAKSAKGGGARQFNGLIDVYRKTLASDGIAGLYR description Mitochondrial matrix => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 66) chain A residue 243-283 type TOPO_DOM sequence TVRRRMMMTSKYKSSIDAFRQIIAKEGVKSLFKGAGA description Mitochondrial matrix => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 67) chain A residue 81-104 type TRANSMEM sequence GNTANVIRYFPTQALNFAFRDKFK description Helical; Name=2 => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI4 68) chain A residue 116-145 type TRANSMEM sequence YAKWMAGNLASGGAAGATSLLFVYSLDYAR description Helical; Name=3 => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI5 69) chain A residue 185-213 type TRANSMEM sequence GFGPSVAGIVVYRGLYFGMYDSIKPVVLV description Helical; Name=4 => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI6 70) chain A residue 217-242 type TRANSMEM sequence ANNFLASFLLGWCVTTGAGIASYPLD description Helical; Name=5 => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI7 71) chain A residue 284-304 type TRANSMEM sequence NILRGVAGAGVLSIYDQLKIL description Helical; Name=6 => ECO:0000269|PubMed:30611538, ECO:0007744|PDB:6GCI source Swiss-Prot : SWS_FT_FI8

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