eF-site ID 1e6e-ABCD PDB Code 1e6e Chain A, B, C, D click to enlarge Title ADRENODOXIN REDUCTASE/ADRENODOXIN COMPLEX OF MITOCHONDRIAL P450 SYSTEMS Classification OXIDOREDUCTASE Compound NADPH\:ADRENODOXIN OXIDOREDUCTASE Source (ADX1_BOVIN) Sequence A:  EQTPQICVVGSGPAGFYTAQHLLKHHSRAHVDIYEKQLVP FGLVRFGVAPDHPEVKNVINTFTQTARSDRCAFYGNVEVG RDVTVQELQDAYHAVVLSYGAEDHQALDIPGEELPGVFSA RAFVGWYNGLPENRELAPDLSCDTAVILGQGNVALDVARI LLTPPDHLEKTDITEAALGALRQSRVKTVWIVGRRGPLQV AFTIKELREMIQLPGTRPMLDPADFLGLQDRIKEAARPRK RLMELLLRTATEKPGVEEAARRASASRAWGLRFFRSPQQV LPSPDGRRAAGIRLAVTRLEGIGEATRAVPTGDVEDLPCG LVLSSIGYKSRPIDPSVPFDPKLGVVPNMEGRVVDVPGLY CSGWVKRGPTGVITTTMTDSFLTGQILLQDLKAGHLPSGP RPGSAFIKALLDSRGVWPVSFSDWEKLDAEEVSRGQASGK PREKLLDPQEMLRLLGH B:  DKITVHFINRDGETLTTKGKIGDSLLDVVVQNNLDIDGFG ACEGTLACSTCHLIFEQHIFEKLEAITDEENDMLDLAYGL TDRSRLGCQICLTKAMDNMTVRVPDAVSDARES C:  QTPQICVVGSGPAGFYTAQHLLKHHSRAHVDIYEKQLVPF GLVRFGVAPDHPEVKNVINTFTQTARSDRCAFYGNVEVGR DVTVQELQDAYHAVVLSYGAEDHQALDIPGEELPGVFSAR AFVGWYNGLPENRELAPDLSCDTAVILGQGNVALDVARIL LTPPDHLEKTDITEAALGALRQSRVKTVWIVGRRGPLQVA FTIKELREMIQLPGTRPMLDPADFLGLQDRIKEAARPRKR LMELLLRTATEKPGVEEAARRASASRAWGLRFFRSPQQVL PSPDGRRAAGIRLAVTRLEGIGEATRAVPTGDVEDLPCGL VLSSIGYKSRPIDPSVPFDPKLGVVPNMEGRVVDVPGLYC SGWVKRGPTGVITTTMTDSFLTGQILLQDLKAGHLPSGPR PGSAFIKALLDSRGVWPVSFSDWEKLDAEEVSRGQASGKP REKLLDPQEMLRLLGH D:  DKITVHFINRDGETLTTKGKIGDSLLDVVVQNNLDIDGFG ACEGTLACSTCHLIFEQHIFEKLEAITDEENDMLDLAYGL TDRSRLGCQICLTKAMDNMTVRVPDA Description Functional site 1) chain A residue 74 type sequence C description BINDING SITE FOR RESIDUE SO4 A 3001 source : AC1 2) chain A residue 76 type sequence F description BINDING SITE FOR RESIDUE SO4 A 3001 source : AC1 3) chain A residue 423 type sequence S description BINDING SITE FOR RESIDUE SO4 A 3001 source : AC1 4) chain A residue 424 type sequence F description BINDING SITE FOR RESIDUE SO4 A 3001 source : AC1 5) chain A residue 425 type sequence S description BINDING SITE FOR RESIDUE SO4 A 3001 source : AC1 6) chain A residue 71 type sequence S description BINDING SITE FOR RESIDUE SO4 A 3004 source : AC2 7) chain A residue 73 type sequence R description BINDING SITE FOR RESIDUE SO4 A 3004 source : AC2 8) chain A residue 334 type sequence R description BINDING SITE FOR RESIDUE SO4 A 3005 source : AC3 9) chain C residue 278 type sequence R description BINDING SITE FOR RESIDUE SO4 A 3005 source : AC3 10) chain C residue 74 type sequence C description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC4 11) chain C residue 76 type sequence F description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC4 12) chain C residue 423 type sequence S description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC4 13) chain C residue 424 type sequence F description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC4 14) chain C residue 425 type sequence S description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC4 15) chain C residue 71 type sequence S description BINDING SITE FOR RESIDUE SO4 C 3003 source : AC5 16) chain C residue 72 type sequence D description BINDING SITE FOR RESIDUE SO4 C 3003 source : AC5 17) chain C residue 73 type sequence R description BINDING SITE FOR RESIDUE SO4 C 3003 source : AC5 18) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 19) chain A residue 15 type sequence G description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 20) chain A residue 16 type sequence P description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 21) chain A residue 17 type sequence A description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 22) chain A residue 38 type sequence E description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 23) chain A residue 39 type sequence K description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 24) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 25) chain A residue 46 type sequence L description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 26) chain A residue 50 type sequence G description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 27) chain A residue 58 type sequence V description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 28) chain A residue 80 type sequence V description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 29) chain A residue 82 type sequence V description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 30) chain A residue 101 type sequence S description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 31) chain A residue 102 type sequence Y description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 32) chain A residue 103 type sequence G description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 33) chain A residue 105 type sequence E description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 34) chain A residue 124 type sequence R description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 35) chain A residue 127 type sequence V description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 36) chain A residue 159 type sequence D description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 37) chain A residue 336 type sequence I description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 38) chain A residue 366 type sequence G description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 39) chain A residue 367 type sequence W description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 40) chain A residue 374 type sequence G description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 41) chain A residue 375 type sequence V description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 42) chain A residue 376 type sequence I description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 43) chain A residue 379 type sequence T description BINDING SITE FOR RESIDUE FAD A 461 source : AC6 44) chain B residue 44 type sequence G description BINDING SITE FOR RESIDUE FES B 129 source : AC7 45) chain B residue 46 type sequence C description BINDING SITE FOR RESIDUE FES B 129 source : AC7 46) chain B residue 48 type sequence G description BINDING SITE FOR RESIDUE FES B 129 source : AC7 47) chain B residue 50 type sequence L description BINDING SITE FOR RESIDUE FES B 129 source : AC7 48) chain B residue 52 type sequence C description BINDING SITE FOR RESIDUE FES B 129 source : AC7 49) chain B residue 55 type sequence C description BINDING SITE FOR RESIDUE FES B 129 source : AC7 50) chain B residue 92 type sequence C description BINDING SITE FOR RESIDUE FES B 129 source : AC7 51) chain C residue 13 type sequence G description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 52) chain C residue 15 type sequence G description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 53) chain C residue 16 type sequence P description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 54) chain C residue 17 type sequence A description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 55) chain C residue 38 type sequence E description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 56) chain C residue 39 type sequence K description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 57) chain C residue 40 type sequence Q description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 58) chain C residue 45 type sequence G description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 59) chain C residue 46 type sequence L description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 60) chain C residue 50 type sequence G description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 61) chain C residue 55 type sequence H description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 62) chain C residue 58 type sequence V description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 63) chain C residue 80 type sequence V description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 64) chain C residue 82 type sequence V description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 65) chain C residue 101 type sequence S description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 66) chain C residue 102 type sequence Y description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 67) chain C residue 103 type sequence G description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 68) chain C residue 105 type sequence E description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 69) chain C residue 159 type sequence D description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 70) chain C residue 336 type sequence I description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 71) chain C residue 366 type sequence G description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 72) chain C residue 367 type sequence W description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 73) chain C residue 374 type sequence G description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 74) chain C residue 375 type sequence V description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 75) chain C residue 376 type sequence I description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 76) chain C residue 379 type sequence T description BINDING SITE FOR RESIDUE FAD C 461 source : AC8 77) chain D residue 44 type sequence G description BINDING SITE FOR RESIDUE FES D 129 source : AC9 78) chain D residue 46 type sequence C description BINDING SITE FOR RESIDUE FES D 129 source : AC9 79) chain D residue 48 type sequence G description BINDING SITE FOR RESIDUE FES D 129 source : AC9 80) chain D residue 50 type sequence L description BINDING SITE FOR RESIDUE FES D 129 source : AC9 81) chain D residue 52 type sequence C description BINDING SITE FOR RESIDUE FES D 129 source : AC9 82) chain D residue 55 type sequence C description BINDING SITE FOR RESIDUE FES D 129 source : AC9 83) chain D residue 92 type sequence C description BINDING SITE FOR RESIDUE FES D 129 source : AC9 84) chain A residue 55 type catalytic sequence H description 142 source MCSA : MCSA1 85) chain A residue 159 type catalytic sequence D description 142 source MCSA : MCSA1 86) chain A residue 376 type catalytic sequence I description 142 source MCSA : MCSA1 87) chain A residue 377 type catalytic sequence T description 142 source MCSA : MCSA1 88) chain C residue 55 type catalytic sequence H description 142 source MCSA : MCSA2 89) chain C residue 159 type catalytic sequence D description 142 source MCSA : MCSA2 90) chain C residue 376 type catalytic sequence I description 142 source MCSA : MCSA2 91) chain C residue 377 type catalytic sequence T description 142 source MCSA : MCSA2 92) chain A residue 209 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI2 93) chain A residue 374 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI2 94) chain C residue 153 type MOD_RES sequence Q description Phosphoserine => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI2 95) chain C residue 197 type MOD_RES sequence R description Phosphoserine => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI2 96) chain C residue 209 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI2 97) chain C residue 374 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI2 98) chain B residue 6 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI3 99) chain D residue 6 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI3 100) chain C residue 279 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI3 101) chain C residue 286 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI3 102) chain B residue 98 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI4 103) chain D residue 98 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P46656 source Swiss-Prot : SWS_FT_FI4 104) chain B residue 117 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10109 source Swiss-Prot : SWS_FT_FI5 105) chain B residue 46-56 type prosite sequence CEGTLACSTCH description ADX Adrenodoxin family, iron-sulfur binding region signature. CegTlACSTCH source prosite : PS00814 106) chain B residue 46 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 107) chain B residue 52 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 108) chain B residue 55 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 109) chain B residue 92 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 110) chain D residue 46 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 111) chain D residue 52 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 112) chain D residue 55 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 113) chain D residue 92 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 114) chain C residue 367 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI1 115) chain C residue 82 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI1

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