eF-site ID 3m4v-AB PDB Code 3m4v Chain A, B click to enlarge Title Crystal structure of the A330P mutant of cytochrome P450 BM3 Classification OXIDOREDUCTASE Compound Bifunctional P-450/NADPH-P450 reductase Source Bacillus megaterium (CPXB_BACME) Sequence A:  MPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEA PGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGD GLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAV QLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNS FYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQ FQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPE TGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNP HVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEALRL WPTAPPFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDK TIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQ FALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGF VVKAKSKKIPL B:  MPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEA PGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGD GLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAV QLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNS FYRDQPHPFITSMVRALDEAMNKLKRQFQEDIKVMNDLVD KIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQ IITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARV LVDPVPSYKQVKQLKYVGMVLNEALRLWPTAPPFSLYAKE DTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPE RFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMM LKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL Description Functional site 1) chain A residue 69 type sequence K description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 2) chain A residue 86 type sequence L description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 3) chain A residue 87 type sequence F description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 4) chain A residue 96 type sequence W description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 5) chain A residue 107 type sequence F description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 6) chain A residue 264 type sequence A description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 7) chain A residue 265 type sequence G description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 8) chain A residue 268 type sequence T description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 9) chain A residue 269 type sequence T description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 10) chain A residue 328 type sequence A description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 11) chain A residue 331 type sequence F description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 12) chain A residue 392 type sequence P description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 13) chain A residue 393 type sequence F description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 14) chain A residue 394 type sequence G description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 15) chain A residue 398 type sequence R description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 16) chain A residue 399 type sequence A description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 17) chain A residue 400 type sequence C description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 18) chain A residue 401 type sequence I description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 19) chain A residue 406 type sequence A description BINDING SITE FOR RESIDUE HEM A 482 source : AC1 20) chain B residue 69 type sequence K description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 21) chain B residue 86 type sequence L description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 22) chain B residue 87 type sequence F description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 23) chain B residue 96 type sequence W description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 24) chain B residue 264 type sequence A description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 25) chain B residue 265 type sequence G description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 26) chain B residue 268 type sequence T description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 27) chain B residue 269 type sequence T description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 28) chain B residue 328 type sequence A description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 29) chain B residue 331 type sequence F description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 30) chain B residue 392 type sequence P description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 31) chain B residue 393 type sequence F description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 32) chain B residue 394 type sequence G description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 33) chain B residue 398 type sequence R description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 34) chain B residue 399 type sequence A description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 35) chain B residue 400 type sequence C description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 36) chain B residue 401 type sequence I description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 37) chain B residue 51 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ source Swiss-Prot : SWS_FT_FI1 38) chain A residue 51 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ source Swiss-Prot : SWS_FT_FI1 39) chain B 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 40) 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 41) 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 42) chain B 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 43) chain A residue 393-402 type prosite sequence FGNGQRACIG description CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGnGQRACIG source prosite : PS00086 44) chain A residue 268 type catalytic sequence T description 699 source MCSA : MCSA1 45) chain A residue 393 type catalytic sequence F description 699 source MCSA : MCSA1 46) chain A residue 400 type catalytic sequence C description 699 source MCSA : MCSA1 47) chain B residue 268 type catalytic sequence T description 699 source MCSA : MCSA2 48) chain B residue 393 type catalytic sequence F description 699 source MCSA : MCSA2 49) chain B residue 400 type catalytic sequence C description 699 source MCSA : MCSA2

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