eF-site ID 1oq7-A PDB Code 1oq7 Chain A 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 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 A residue 77 type sequence D description BINDING SITE FOR RESIDUE SR B 365 source : AC4 4) chain A residue 62 type catalytic sequence W description 136 source MCSA : MCSA1 5) chain A residue 105 type catalytic sequence E description 136 source MCSA : MCSA1 6) chain A residue 143 type catalytic sequence E description 136 source MCSA : MCSA1 7) chain A residue 146 type catalytic sequence H description 136 source MCSA : MCSA1 8) chain A residue 196 type catalytic sequence E description 136 source MCSA : MCSA1 9) chain A residue 199 type catalytic sequence T description 136 source MCSA : MCSA1 10) chain A residue 228 type catalytic sequence D description 136 source MCSA : MCSA1 11) chain A residue 229 type catalytic sequence E description 136 source MCSA : MCSA1 12) chain A residue 232 type catalytic sequence H description 136 source MCSA : MCSA1 13) 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 14) 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 15) 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 16) 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 17) 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 18) 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 19) 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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