eF-site ID 1oq4-B PDB Code 1oq4 Chain B 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 null (STAD_RICCO) Sequence B:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL EERAQGRAKEAPTMPFSWIFDRQVKL Description Functional site 1) chain B residue 105 type sequence E description BINDING SITE FOR RESIDUE FE B 364 source : AC4 2) chain B residue 143 type sequence E description BINDING SITE FOR RESIDUE FE B 364 source : AC4 3) chain B residue 146 type sequence H description BINDING SITE FOR RESIDUE FE B 364 source : AC4 4) chain B residue 229 type sequence E description BINDING SITE FOR RESIDUE FE B 364 source : AC4 5) chain B residue 143 type sequence E description BINDING SITE FOR RESIDUE FE B 365 source : AC5 6) chain B residue 196 type sequence E description BINDING SITE FOR RESIDUE FE B 365 source : AC5 7) chain B residue 229 type sequence E description BINDING SITE FOR RESIDUE FE B 365 source : AC5 8) chain B residue 232 type sequence H description BINDING SITE FOR RESIDUE FE B 365 source : AC5 9) chain B residue 105 type sequence E description BINDING SITE FOR RESIDUE AZI B 1366 source : AC6 10) chain B residue 143 type sequence E description BINDING SITE FOR RESIDUE AZI B 1366 source : AC6 11) chain B residue 196 type sequence E description BINDING SITE FOR RESIDUE AZI B 1366 source : AC6 12) chain B residue 199 type sequence T description BINDING SITE FOR RESIDUE AZI B 1366 source : AC6 13) 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 14) 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 15) 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 16) 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 17) 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 18) 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 19) chain B residue 62 type catalytic sequence W description 136 source MCSA : MCSA2 20) chain B residue 105 type catalytic sequence E description 136 source MCSA : MCSA2 21) chain B residue 143 type catalytic sequence E description 136 source MCSA : MCSA2 22) chain B residue 146 type catalytic sequence H description 136 source MCSA : MCSA2 23) chain B residue 196 type catalytic sequence E description 136 source MCSA : MCSA2 24) chain B residue 199 type catalytic sequence T description 136 source MCSA : MCSA2 25) chain B residue 228 type catalytic sequence D description 136 source MCSA : MCSA2 26) chain B residue 229 type catalytic sequence E description 136 source MCSA : MCSA2 27) chain B residue 232 type catalytic sequence H description 136 source MCSA : MCSA2

Display surface Download Links