eF-site ID 1oq7-ABEF PDB Code 1oq7 Chain A, B, E, F click to enlarge Title The crystal structure of the iron free (Apo-)form of Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean). Classification OXIDOREDUCTASE Compound Acyl-[acyl-carrier protein] desaturase Source Ricinus communis (Castor bean) (STAD_RICCO) Sequence A:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL EERAQGRAKEAPTMPFSWIFDRQVKL B:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL EERAQGRAKEAPTMPFSWIFDRQVKL E:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL EERAQGRAKEAPTMPFSWIFDRQVKL F:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL EERAQGRAKEAPTMPFSWIFDRQVKL Description Functional site 1) chain A residue 106 type sequence E description BINDING SITE FOR RESIDUE SR B 364 source : AC1 2) chain A residue 148 type sequence D description BINDING SITE FOR RESIDUE SR B 364 source : AC1 3) chain B residue 106 type sequence E description BINDING SITE FOR RESIDUE SR B 364 source : AC1 4) chain B residue 148 type sequence D description BINDING SITE FOR RESIDUE SR B 364 source : AC1 5) chain E residue 106 type sequence E description BINDING SITE FOR RESIDUE SR E 364 source : AC3 6) chain E residue 148 type sequence D description BINDING SITE FOR RESIDUE SR E 364 source : AC3 7) chain F residue 106 type sequence E description BINDING SITE FOR RESIDUE SR E 364 source : AC3 8) chain A residue 77 type sequence D description BINDING SITE FOR RESIDUE SR B 365 source : AC4 9) chain B residue 77 type sequence D description BINDING SITE FOR RESIDUE SR B 365 source : AC4 10) chain E residue 77 type sequence D description BINDING SITE FOR RESIDUE SR F 364 source : AC6 11) chain F residue 77 type sequence D description BINDING SITE FOR RESIDUE SR F 364 source : AC6 12) chain B residue 70 type sequence D description BINDING SITE FOR RESIDUE SR A 364 source : AC7 13) chain A residue 62 type catalytic sequence W description 136 source MCSA : MCSA1 14) chain A residue 105 type catalytic sequence E description 136 source MCSA : MCSA1 15) chain A residue 143 type catalytic sequence E description 136 source MCSA : MCSA1 16) chain A residue 146 type catalytic sequence H description 136 source MCSA : MCSA1 17) chain A residue 196 type catalytic sequence E description 136 source MCSA : MCSA1 18) chain A residue 199 type catalytic sequence T description 136 source MCSA : MCSA1 19) chain A residue 228 type catalytic sequence D description 136 source MCSA : MCSA1 20) chain A residue 229 type catalytic sequence E description 136 source MCSA : MCSA1 21) chain A residue 232 type catalytic sequence H description 136 source MCSA : MCSA1 22) chain B residue 62 type catalytic sequence W description 136 source MCSA : MCSA2 23) chain B residue 105 type catalytic sequence E description 136 source MCSA : MCSA2 24) chain B residue 143 type catalytic sequence E description 136 source MCSA : MCSA2 25) chain B residue 146 type catalytic sequence H description 136 source MCSA : MCSA2 26) chain B residue 196 type catalytic sequence E description 136 source MCSA : MCSA2 27) chain B residue 199 type catalytic sequence T description 136 source MCSA : MCSA2 28) chain B residue 228 type catalytic sequence D description 136 source MCSA : MCSA2 29) chain B residue 229 type catalytic sequence E description 136 source MCSA : MCSA2 30) chain B residue 232 type catalytic sequence H description 136 source MCSA : MCSA2 31) chain E residue 62 type catalytic sequence W description 136 source MCSA : MCSA5 32) chain E residue 105 type catalytic sequence E description 136 source MCSA : MCSA5 33) chain E residue 143 type catalytic sequence E description 136 source MCSA : MCSA5 34) chain E residue 146 type catalytic sequence H description 136 source MCSA : MCSA5 35) chain E residue 196 type catalytic sequence E description 136 source MCSA : MCSA5 36) chain E residue 199 type catalytic sequence T description 136 source MCSA : MCSA5 37) chain E residue 228 type catalytic sequence D description 136 source MCSA : MCSA5 38) chain E residue 229 type catalytic sequence E description 136 source MCSA : MCSA5 39) chain E residue 232 type catalytic sequence H description 136 source MCSA : MCSA5 40) chain F residue 62 type catalytic sequence W description 136 source MCSA : MCSA6 41) chain F residue 105 type catalytic sequence E description 136 source MCSA : MCSA6 42) chain F residue 143 type catalytic sequence E description 136 source MCSA : MCSA6 43) chain F residue 146 type catalytic sequence H description 136 source MCSA : MCSA6 44) chain F residue 196 type catalytic sequence E description 136 source MCSA : MCSA6 45) chain F residue 199 type catalytic sequence T description 136 source MCSA : MCSA6 46) chain F residue 228 type catalytic sequence D description 136 source MCSA : MCSA6 47) chain F residue 229 type catalytic sequence E description 136 source MCSA : MCSA6 48) chain F residue 232 type catalytic sequence H description 136 source MCSA : MCSA6 49) chain A residue 105 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 50) chain B residue 196 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 51) chain B residue 229 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 52) chain B residue 232 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 143 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 54) chain E residue 105 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 55) chain E residue 143 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 56) chain E residue 146 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 57) chain E residue 196 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 58) chain E residue 229 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 59) chain A residue 146 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 60) chain E residue 232 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 61) chain F residue 105 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 62) chain F residue 143 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 63) chain F residue 146 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 64) chain F residue 196 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 65) chain F residue 229 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 66) chain F residue 232 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 67) chain A residue 196 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 68) chain A residue 229 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 69) chain A residue 232 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 70) chain B residue 105 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 71) chain B residue 143 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 72) chain B residue 146 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 283-302 type prosite sequence SAVAQRLGVYTAKDYADILE description FATTY_ACID_DESATUR_2 Fatty acid desaturases family 2 signature. SAvaqRLgvytakDYadILE source prosite : PS00574

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