eF-site ID 3psx-B PDB Code 3psx Chain B click to enlarge Title Crystal structure of the KT2 mutant of cytochrome P450 BM3 Classification OXIDOREDUCTASE Compound Bifunctional P-450/NADPH-P450 reductase Source Bacillus megaterium (CPXB_BACME) Sequence B:  MPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEA PGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGD GLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAV QLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNS FYRDQPHPFITMNDLVDKIIADRKASQSDDLLTHMLHGKD PETGEPLDDENIRYQIVTFLIAGHETTSGLLSFTLYFLVK NPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEAL RLWPTAPAFSLYAKEDTVLGGEYPLEKGDEIMVLIPQLHR DKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIG QQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPE GFVVKAKSKKIPLG Description Functional site 1) chain B residue 69 type sequence K description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 2) chain B residue 86 type sequence L description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 3) chain B residue 87 type sequence F description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 4) chain B residue 96 type sequence W description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 5) chain B residue 107 type sequence F description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 6) chain B residue 261 type sequence F description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 7) chain B residue 264 type sequence A description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 8) chain B residue 265 type sequence G description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 9) chain B residue 268 type sequence T description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 10) chain B residue 269 type sequence T description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 11) chain B residue 272 type sequence L description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 12) chain B residue 327 type sequence T description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 13) chain B residue 331 type sequence F description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 14) chain B residue 392 type sequence P description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 15) chain B residue 393 type sequence F description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 16) chain B residue 394 type sequence G description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 17) chain B residue 398 type sequence R description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 18) chain B residue 399 type sequence A description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 19) chain B residue 400 type sequence C description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 20) chain B residue 401 type sequence I description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 21) chain B residue 402 type sequence G description BINDING SITE FOR RESIDUE HEM B 482 source : AC2 22) chain B residue 51 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ source Swiss-Prot : SWS_FT_FI1 23) 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 24) chain B residue 268 type catalytic sequence T description 699 source MCSA : MCSA2 25) chain B residue 393 type catalytic sequence F description 699 source MCSA : MCSA2 26) chain B residue 400 type catalytic sequence C description 699 source MCSA : MCSA2 27) 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

Display surface Download Links