eF-site ID 6h1o-A PDB Code 6h1o Chain A click to enlarge Title Structure of the BM3 heme domain in complex with voriconazole Classification OXIDOREDUCTASE Compound Bifunctional cytochrome P450/NADPH--P450 reductase Source (CPXB_BACMB) Sequence A:  IKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFK FEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDF FGDGLVTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVD IAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYR FNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDEN KRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGK DPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLV KNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEA LRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLH RDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACI GQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKP EGFVVKAKSKKIPLGG Description Functional site 1) chain A residue 69 type sequence K description binding site for residue HEM A 501 source : AC1 2) chain A residue 75 type sequence L description binding site for residue HEM A 501 source : AC1 3) chain A residue 86 type sequence L description binding site for residue HEM A 501 source : AC1 4) chain A residue 87 type sequence V description binding site for residue HEM A 501 source : AC1 5) chain A residue 96 type sequence W description binding site for residue HEM A 501 source : AC1 6) chain A residue 107 type sequence F description binding site for residue HEM A 501 source : AC1 7) chain A residue 261 type sequence F description binding site for residue HEM A 501 source : AC1 8) chain A residue 264 type sequence A description binding site for residue HEM A 501 source : AC1 9) chain A residue 265 type sequence G description binding site for residue HEM A 501 source : AC1 10) chain A residue 268 type sequence T description binding site for residue HEM A 501 source : AC1 11) chain A residue 269 type sequence T description binding site for residue HEM A 501 source : AC1 12) chain A residue 327 type sequence T description binding site for residue HEM A 501 source : AC1 13) chain A residue 331 type sequence F description binding site for residue HEM A 501 source : AC1 14) chain A residue 392 type sequence P description binding site for residue HEM A 501 source : AC1 15) chain A residue 393 type sequence F description binding site for residue HEM A 501 source : AC1 16) chain A residue 394 type sequence G description binding site for residue HEM A 501 source : AC1 17) chain A residue 398 type sequence R description binding site for residue HEM A 501 source : AC1 18) chain A residue 399 type sequence A description binding site for residue HEM A 501 source : AC1 19) chain A residue 400 type sequence C description binding site for residue HEM A 501 source : AC1 20) chain A residue 401 type sequence I description binding site for residue HEM A 501 source : AC1 21) chain A residue 402 type sequence G description binding site for residue HEM A 501 source : AC1 22) chain A residue 406 type sequence A description binding site for residue HEM A 501 source : AC1 23) chain A residue 82 type sequence F description binding site for residue VOR A 502 source : AC2 24) chain A residue 87 type sequence V description binding site for residue VOR A 502 source : AC2 25) chain A residue 260 type sequence T description binding site for residue VOR A 502 source : AC2 26) chain A residue 263 type sequence I description binding site for residue VOR A 502 source : AC2 27) chain A residue 264 type sequence A description binding site for residue VOR A 502 source : AC2 28) chain A residue 267 type sequence E description binding site for residue VOR A 502 source : AC2 29) chain A residue 268 type sequence T description binding site for residue VOR A 502 source : AC2 30) chain A residue 366 type sequence I description binding site for residue PO4 A 503 source : AC3 31) chain A residue 378 type sequence R description binding site for residue PO4 A 503 source : AC3 32) chain A residue 384 type sequence A description binding site for residue PO4 A 503 source : AC3 33) chain A residue 281 type sequence V description binding site for residue PO4 A 504 source : AC4 34) chain A residue 282 type sequence K description binding site for residue PO4 A 504 source : AC4 35) chain A residue 425 type sequence D description binding site for residue PO4 A 504 source : AC4 36) chain A residue 137 type sequence E description binding site for residue PO4 A 505 source : AC5 37) chain A residue 138 type sequence H description binding site for residue PO4 A 505 source : AC5 38) chain A residue 97 type sequence K description binding site for residue GOL A 506 source : AC6 39) chain A residue 100 type sequence H description binding site for residue GOL A 506 source : AC6 40) chain A residue 101 type sequence N description binding site for residue GOL A 506 source : AC6 41) chain A residue 132 type sequence R description binding site for residue GOL A 507 source : AC7 42) chain A residue 75 type sequence L description binding site for residue GOL A 508 source : AC8 43) chain A residue 330 type sequence A description binding site for residue GOL A 508 source : AC8 44) chain A residue 81 type sequence F description binding site for residue EDO A 509 source : AC9 45) chain A residue 213 type sequence N description binding site for residue EDO A 509 source : AC9 46) chain A residue 259 type sequence I description binding site for residue EDO A 509 source : AC9 47) chain A residue 4 type sequence E description binding site for residue PO4 B 504 source : AD4 48) chain A residue 51 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ source Swiss-Prot : SWS_FT_FI1 49) chain A residue 268 type catalytic sequence T description 699 source MCSA : MCSA1 50) chain A residue 393 type catalytic sequence F description 699 source MCSA : MCSA1 51) chain A residue 400 type catalytic sequence C description 699 source MCSA : MCSA1 52) chain A residue 268 type SITE sequence T description Important for catalytic activity => ECO:0000305|PubMed:16403573, ECO:0000305|PubMed:7578081 source Swiss-Prot : SWS_FT_FI3 53) chain A residue 393-402 type prosite sequence FGNGQRACIG description CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGnGQRACIG source prosite : PS00086 54) chain A residue 400 type BINDING sequence C description axial binding residue => ECO:0000269|PubMed:10051560, ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:15020590, ECO:0000269|PubMed:15299332, ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:17077084, ECO:0000269|PubMed:17429965, ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466, ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:20947800, ECO:0000269|PubMed:21110374, ECO:0000269|PubMed:21875028, ECO:0000269|PubMed:7578081, ECO:0000269|PubMed:8342039, ECO:0000269|PubMed:9033595, ECO:0007744|PDB:1BU7, ECO:0007744|PDB:1BVY, ECO:0007744|PDB:1FAG, ECO:0007744|PDB:1FAH, ECO:0007744|PDB:1JME, ECO:0007744|PDB:1JPZ, ECO:0007744|PDB:1P0V, ECO:0007744|PDB:1P0W, ECO:0007744|PDB:1P0X, ECO:0007744|PDB:1SMI, ECO:0007744|PDB:1SMJ, ECO:0007744|PDB:1YQO, ECO:0007744|PDB:1YQP, ECO:0007744|PDB:1ZO4, ECO:0007744|PDB:1ZO9, ECO:0007744|PDB:1ZOA, ECO:0007744|PDB:2BMH, ECO:0007744|PDB:2HPD, ECO:0007744|PDB:2IJ2, ECO:0007744|PDB:2IJ3, ECO:0007744|PDB:2IJ4, ECO:0007744|PDB:2J1M, ECO:0007744|PDB:2J4S, ECO:0007744|PDB:2UWH, ECO:0007744|PDB:3BEN, ECO:0007744|PDB:3CBD, ECO:0007744|PDB:3EKB, ECO:0007744|PDB:3EKD, ECO:0007744|PDB:3EKF, ECO:0007744|PDB:3HF2, ECO:0007744|PDB:3KX3, ECO:0007744|PDB:3KX4, ECO:0007744|PDB:3KX5, ECO:0007744|PDB:3M4V, ECO:0007744|PDB:3NPL source Swiss-Prot : SWS_FT_FI2

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