eF-site ID 3psx-AB
PDB Code 3psx
Chain A, B

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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 A:  EMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFE
APGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAG
DGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIA
VQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFN
SFYRDQPHPVMNDLVDKIIADRKASQSDDLLTHMLHGKDP
ETGEPLDDENIRYQIVTFLIAGHETTSGLLSFTLYFLVKN
PHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEALR
LWPTAPAFSLYAKEDTVLGGEYPLEKGDEIMVLIPQLHRD
KTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQ
QFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEG
FVVKAKSKKIPL
B:  MPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEA
PGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGD
GLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAV
QLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNS
FYRDQPHPFITMNDLVDKIIADRKASQSDDLLTHMLHGKD
PETGEPLDDENIRYQIVTFLIAGHETTSGLLSFTLYFLVK
NPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEAL
RLWPTAPAFSLYAKEDTVLGGEYPLEKGDEIMVLIPQLHR
DKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIG
QQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPE
GFVVKAKSKKIPLG
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 264
type
sequence A
description BINDING SITE FOR RESIDUE HEM A 482
source : AC1

6) chain A
residue 265
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 482
source : AC1

7) chain A
residue 268
type
sequence T
description BINDING SITE FOR RESIDUE HEM A 482
source : AC1

8) chain A
residue 269
type
sequence T
description BINDING SITE FOR RESIDUE HEM A 482
source : AC1

9) chain A
residue 322
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 482
source : AC1

10) chain A
residue 327
type
sequence T
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 402
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 482
source : AC1

20) chain A
residue 405
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 482
source : AC1

21) chain A
residue 406
type
sequence A
description BINDING SITE FOR RESIDUE HEM A 482
source : AC1

22) chain B
residue 69
type
sequence K
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

23) chain B
residue 86
type
sequence L
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

24) chain B
residue 87
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

25) chain B
residue 96
type
sequence W
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

26) chain B
residue 107
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

27) chain B
residue 261
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

28) chain B
residue 264
type
sequence A
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

29) chain B
residue 265
type
sequence G
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

30) chain B
residue 268
type
sequence T
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

31) chain B
residue 269
type
sequence T
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

32) chain B
residue 272
type
sequence L
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

33) chain B
residue 327
type
sequence T
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

34) chain B
residue 331
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

35) chain B
residue 392
type
sequence P
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

36) chain B
residue 393
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

37) chain B
residue 394
type
sequence G
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

38) chain B
residue 398
type
sequence R
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

39) chain B
residue 399
type
sequence A
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

40) chain B
residue 400
type
sequence C
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

41) chain B
residue 401
type
sequence I
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

42) chain B
residue 402
type
sequence G
description BINDING SITE FOR RESIDUE HEM B 482
source : AC2

43) chain A
residue 268
type catalytic
sequence T
description 699
source MCSA : MCSA1

44) chain A
residue 393
type catalytic
sequence F
description 699
source MCSA : MCSA1

45) chain A
residue 400
type catalytic
sequence C
description 699
source MCSA : MCSA1

46) chain B
residue 268
type catalytic
sequence T
description 699
source MCSA : MCSA2

47) chain B
residue 393
type catalytic
sequence F
description 699
source MCSA : MCSA2

48) chain B
residue 400
type catalytic
sequence C
description 699
source MCSA : MCSA2

49) chain A
residue 393-402
type prosite
sequence FGNGQRACIG
description CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGnGQRACIG
source prosite : PS00086

50) chain A
residue 51
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ
source Swiss-Prot : SWS_FT_FI1

51) chain B
residue 51
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ
source Swiss-Prot : SWS_FT_FI1

52) 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

53) 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

54) 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

55) 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


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