eF-site ID 1oq4-D PDB Code 1oq4 Chain D click to enlarge Title The Crystal Structure of the Complex between Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean) and Azide. Classification OXIDOREDUCTASE Compound Acyl-[acyl-carrier protein] desaturase Source Ricinus communis (Castor bean) (STAD_RICCO) Sequence D:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL EERAQGRAKEAPTMPFSWIFDRQVKL Description Functional site 1) chain D residue 105 type sequence E description BINDING SITE FOR RESIDUE FE D 364 source : BC1 2) chain D residue 143 type sequence E description BINDING SITE FOR RESIDUE FE D 364 source : BC1 3) chain D residue 146 type sequence H description BINDING SITE FOR RESIDUE FE D 364 source : BC1 4) chain D residue 229 type sequence E description BINDING SITE FOR RESIDUE FE D 364 source : BC1 5) chain D residue 143 type sequence E description BINDING SITE FOR RESIDUE FE D 365 source : BC2 6) chain D residue 196 type sequence E description BINDING SITE FOR RESIDUE FE D 365 source : BC2 7) chain D residue 229 type sequence E description BINDING SITE FOR RESIDUE FE D 365 source : BC2 8) chain D residue 232 type sequence H description BINDING SITE FOR RESIDUE FE D 365 source : BC2 9) chain D residue 105 type sequence E description BINDING SITE FOR RESIDUE AZI D 3366 source : BC3 10) chain D residue 143 type sequence E description BINDING SITE FOR RESIDUE AZI D 3366 source : BC3 11) chain D residue 196 type sequence E description BINDING SITE FOR RESIDUE AZI D 3366 source : BC3 12) chain D residue 199 type sequence T description BINDING SITE FOR RESIDUE AZI D 3366 source : BC3 13) chain D residue 62 type catalytic sequence W description 136 source MCSA : MCSA4 14) chain D residue 105 type catalytic sequence E description 136 source MCSA : MCSA4 15) chain D residue 143 type catalytic sequence E description 136 source MCSA : MCSA4 16) chain D residue 146 type catalytic sequence H description 136 source MCSA : MCSA4 17) chain D residue 196 type catalytic sequence E description 136 source MCSA : MCSA4 18) chain D residue 199 type catalytic sequence T description 136 source MCSA : MCSA4 19) chain D residue 228 type catalytic sequence D description 136 source MCSA : MCSA4 20) chain D residue 229 type catalytic sequence E description 136 source MCSA : MCSA4 21) chain D residue 232 type catalytic sequence H description 136 source MCSA : MCSA4 22) chain D 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 23) chain D 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 24) chain D 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 25) chain D 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 26) chain D 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 27) chain D 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

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