eF-site ID 1afr-C PDB Code 1afr Chain C click to enlarge Title STEAROYL-ACYL CARRIER PROTEIN DESATURASE FROM CASTOR SEEDS Classification OXIDOREDUCTASE Compound DELTA9 STEAROYL-ACYL CARRIER PROTEIN DESATURASE Source (STAD_RICCO) Sequence C:  MPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKPV EKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVVL VGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTRA WTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMD PRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIKL AQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFADM MRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDYA DILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRLE ERAQGRAKEAPTMPFSWIFDRQVKL Description Functional site 1) chain C residue 143 type sequence E description BINDING SITE FOR RESIDUE FE2 C 558 source : AC5 2) chain C residue 196 type sequence E description BINDING SITE FOR RESIDUE FE2 C 558 source : AC5 3) chain C residue 229 type sequence E description BINDING SITE FOR RESIDUE FE2 C 558 source : AC5 4) chain C residue 232 type sequence H description BINDING SITE FOR RESIDUE FE2 C 558 source : AC5 5) chain C residue 105 type sequence E description BINDING SITE FOR RESIDUE FE2 C 559 source : AC6 6) chain C residue 143 type sequence E description BINDING SITE FOR RESIDUE FE2 C 559 source : AC6 7) chain C residue 146 type sequence H description BINDING SITE FOR RESIDUE FE2 C 559 source : AC6 8) chain C residue 229 type sequence E description BINDING SITE FOR RESIDUE FE2 C 559 source : AC6 9) chain C residue 62 type catalytic sequence W description 136 source MCSA : MCSA3 10) chain C residue 105 type catalytic sequence E description 136 source MCSA : MCSA3 11) chain C residue 143 type catalytic sequence E description 136 source MCSA : MCSA3 12) chain C residue 146 type catalytic sequence H description 136 source MCSA : MCSA3 13) chain C residue 196 type catalytic sequence E description 136 source MCSA : MCSA3 14) chain C residue 199 type catalytic sequence T description 136 source MCSA : MCSA3 15) chain C residue 228 type catalytic sequence D description 136 source MCSA : MCSA3 16) chain C residue 229 type catalytic sequence E description 136 source MCSA : MCSA3 17) chain C residue 232 type catalytic sequence H description 136 source MCSA : MCSA3 18) chain C 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 19) chain C 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 20) chain C 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 21) chain C 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 22) chain C 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 23) chain C 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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