eF-site ID 1di1-A PDB Code 1di1 Chain A click to enlarge Title CRYSTAL STRUCTURE OF ARISTOLOCHENE SYNTHASE FROM PENICILLIUM ROQUEFORTI Classification LYASE Compound ARISTOLOCHENE SYNTHASE Source (ARIS_PENRO) Sequence A:  TPPPTQWSYLCHPRVKEVQDEVDGYFLENWKFPSFKAVRT FLDAKFSEVTCLYFPLALDDRIHFACRLLTVLFLIDDVLE HMSFADGEAYNNRLIPISRGDVLPDRTKPEEFILYDLWES MRAHDAELANEVLEPTFVFMRAQTDRARLSIHELGHYLEY REKDVGKALLSALMRFSMGLRLSADELQDMKALEANCAKQ LSVVNDIYSYDKEEEALCSAVKVLAEESKLGIPATKRVLW SMTREWETVHDEIVAEKIASPDGCSEAAKAYMKGLEYQMS GNEQWSKTTR Description Functional site 1) chain A residue 92 type catalytic sequence Y description 261 source MCSA : MCSA1 2) chain A residue 112 type catalytic sequence F description 261 source MCSA : MCSA1 3) chain A residue 178 type catalytic sequence F description 261 source MCSA : MCSA1 4) chain A residue 206 type catalytic sequence K description 261 source MCSA : MCSA1 5) chain A residue 333 type catalytic sequence W description 261 source MCSA : MCSA1 6) chain A residue 115 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10825154, ECO:0007744|PDB:1DGP source Swiss-Prot : SWS_FT_FI1 7) chain A residue 244 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10825154, ECO:0007744|PDB:1DGP source Swiss-Prot : SWS_FT_FI1 8) chain A residue 200 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q9UR08 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 248 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q9UR08 source Swiss-Prot : SWS_FT_FI2 10) chain A residue 251 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q9UR08 source Swiss-Prot : SWS_FT_FI2 11) chain A residue 252 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9UR08 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 112 type SITE sequence F description Important for catalytic activity => ECO:0000269|PubMed:10825154, ECO:0007744|PDB:1DI1 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 178 type SITE sequence F description Important for catalytic activity => ECO:0000269|PubMed:10825154, ECO:0007744|PDB:1DI1 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 333 type SITE sequence W description Important for catalytic activity => ECO:0000269|PubMed:10825154, ECO:0007744|PDB:1DI1 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 92 type SITE sequence Y description Important for catalytic activity => ECO:0000269|PubMed:10825154, ECO:0007744|PDB:1DI1 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 188-197 type prosite sequence LSIHELGHYL description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. LSIHELGHYL source prosite : PS00142

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