eF-site ID 1b4v-A PDB Code 1b4v Chain A click to enlarge Title CHOLESTEROL OXIDASE FROM STREPTOMYCES Classification OXIDOREDUCTASE Compound PROTEIN (CHOLESTEROL OXIDASE) Source ORGANISM_SCIENTIFIC: Streptomyces sp.; Sequence A:  GYVPAVVIGTGYGAAVSALRLGEAGVQTLMLEMGQLWNQP GPDGNIFCGMLNPDKRSSWFKNRTEAPLGSFLWLDVVNRN IDPYAGVLDRVNYDQMSVYVGRGVGGGSLVNGGMAVEPKR SYFEEILPRVDSSEMYDRYFPRANSMLRVNHIDTKWFEDT EWYKFARVSREQAGKAGLGTVFVPNVYDFGYMQREAAGEV PKSALATEVIYGNNHGKQSLDKTYLAAALGTGKVTIQTLH QVKTIRQTKDGGYALTVEQKDTDGKLLATKEISCRYLFLG AGSLGSTELLVRARDTGTLPNLNSEVGAGWGPNGNIMTAR ANHMWNPTGAHQSSIPALGIDAWDNSDSSVFAEIAPMPAG LETWVSLYLAITKNPQRGTFVYDAATDRAKLNWTRDQNAP AVNAAKALFDRINKANGTIYRYDLFGTQLKAFADDFCYHP LGGCVLGKATDDYGRVAGYKNLYVTDGSLIPGSVGVNPFV TITALAERNVERIIKQDV Description Functional site 1) chain A residue 447 type sequence H description HISTIDINE 447 IS PRESUMED TO BE THE ACTIVE SITE BASE IN THE OXIDASE REACTION. THE BASE CATALYZED MECHANISM IS MEDIATED THROUGH A WATER MOLECULE AT POSITION 541. GLU 361 IS THE BASE IN THE ISOMERIZATION REACTION. ASN 485 IS BELIEVED TO BE INVOLVED IN POSITIONING THE WATER MOLECULE. source : CAT 2) chain A residue 361 type sequence E description HISTIDINE 447 IS PRESUMED TO BE THE ACTIVE SITE BASE IN THE OXIDASE REACTION. THE BASE CATALYZED MECHANISM IS MEDIATED THROUGH A WATER MOLECULE AT POSITION 541. GLU 361 IS THE BASE IN THE ISOMERIZATION REACTION. ASN 485 IS BELIEVED TO BE INVOLVED IN POSITIONING THE WATER MOLECULE. source : CAT 3) chain A residue 485 type sequence N description HISTIDINE 447 IS PRESUMED TO BE THE ACTIVE SITE BASE IN THE OXIDASE REACTION. THE BASE CATALYZED MECHANISM IS MEDIATED THROUGH A WATER MOLECULE AT POSITION 541. GLU 361 IS THE BASE IN THE ISOMERIZATION REACTION. ASN 485 IS BELIEVED TO BE INVOLVED IN POSITIONING THE WATER MOLECULE. source : CAT 4) chain A residue 16 type sequence I description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 5) chain A residue 17 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 6) chain A residue 19 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 7) chain A residue 20 type sequence Y description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 8) chain A residue 21 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 9) chain A residue 39 type sequence L description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 10) chain A residue 40 type sequence E description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 11) chain A residue 41 type sequence M description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 12) chain A residue 107 type sequence Y description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 13) chain A residue 109 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 14) chain A residue 110 type sequence R description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 15) chain A residue 111 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 16) chain A residue 114 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 17) chain A residue 115 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 18) chain A residue 119 type sequence N description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 19) chain A residue 120 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 20) chain A residue 121 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 21) chain A residue 122 type sequence M description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 22) chain A residue 218 type sequence I description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 23) chain A residue 248 type sequence H description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 24) chain A residue 249 type sequence Q description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 25) chain A residue 250 type sequence V description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 26) chain A residue 288 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 27) chain A residue 289 type sequence A description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 28) chain A residue 290 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 29) chain A residue 446 type sequence Y description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 30) chain A residue 447 type sequence H description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 31) chain A residue 474 type sequence D description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 32) chain A residue 475 type sequence G description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 33) chain A residue 485 type sequence N description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 34) chain A residue 486 type sequence P description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 35) chain A residue 487 type sequence F description BINDING SITE FOR RESIDUE FAD A 510 source : AC1 36) chain A residue 109-132 type prosite sequence GRGVGGGSLVNGGMAVEPKRSYFE description GMC_OXRED_1 GMC oxidoreductases signature 1. GRgVGGGSlVNggmAvePkrsyfE source prosite : PS00623 37) chain A residue 361 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:10194345 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 447 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:10194345 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 20 type BINDING sequence Y description BINDING => ECO:0007744|PDB:1B4V source Swiss-Prot : SWS_FT_FI2 40) chain A residue 40 type BINDING sequence E description BINDING => ECO:0007744|PDB:1B4V source Swiss-Prot : SWS_FT_FI2 41) chain A residue 115 type BINDING sequence G description BINDING => ECO:0007744|PDB:1B4V source Swiss-Prot : SWS_FT_FI2 42) chain A residue 119 type BINDING sequence N description BINDING => ECO:0007744|PDB:1B4V source Swiss-Prot : SWS_FT_FI2 43) chain A residue 250 type BINDING sequence V description BINDING => ECO:0007744|PDB:1B4V source Swiss-Prot : SWS_FT_FI2 44) chain A residue 475 type BINDING sequence G description BINDING => ECO:0007744|PDB:1B4V source Swiss-Prot : SWS_FT_FI2 45) chain A residue 487 type BINDING sequence F description BINDING => ECO:0007744|PDB:1B4V source Swiss-Prot : SWS_FT_FI2 46) chain A residue 446 type BINDING sequence Y description BINDING => ECO:0007744|PDB:1IJH source Swiss-Prot : SWS_FT_FI3

Display surface Download Links