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