|
eF-site ID
|
1p0w-B |
PDB Code
|
1p0w |
Chain
|
B |
|
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|
|
Title
|
F393W mutant heme domain of flavocytochrome P450 BM3 |
Classification
|
OXIDOREDUCTASE |
Compound
|
Bifunctional P-450:NADPH-P450 reductase |
Source
|
Bacillus megaterium (CPXB_BACME) |
|
Sequence
|
B: |
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKF
EAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFA
GDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDI
AVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRF
NSFYRDQPHPFITSMVRALDEAMNKLQRPAYDENKRQFQE
DIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGE
PLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVL
QKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEALRLWPT
APAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIW
GDDVEEFRPERFENPSAIPQHAFKPWGNGQRACIGQQFAL
HEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVK
AKSKKIPL
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
B |
residue |
69 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
2)
|
chain |
B |
residue |
86 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
3)
|
chain |
B |
residue |
87 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
4)
|
chain |
B |
residue |
96 |
type |
|
sequence |
W
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
5)
|
chain |
B |
residue |
264 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
6)
|
chain |
B |
residue |
265 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
7)
|
chain |
B |
residue |
268 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
8)
|
chain |
B |
residue |
269 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
9)
|
chain |
B |
residue |
327 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
10)
|
chain |
B |
residue |
331 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
11)
|
chain |
B |
residue |
392 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
12)
|
chain |
B |
residue |
393 |
type |
|
sequence |
W
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
13)
|
chain |
B |
residue |
394 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
14)
|
chain |
B |
residue |
398 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
15)
|
chain |
B |
residue |
399 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
16)
|
chain |
B |
residue |
400 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
17)
|
chain |
B |
residue |
401 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
18)
|
chain |
B |
residue |
402 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE HEM B 460
|
source |
: AC2
|
|
19)
|
chain |
B |
residue |
269 |
type |
catalytic |
sequence |
T
|
description |
699
|
source |
MCSA : MCSA2
|
|
20)
|
chain |
B |
residue |
394 |
type |
catalytic |
sequence |
G
|
description |
699
|
source |
MCSA : MCSA2
|
|
21)
|
chain |
B |
residue |
401 |
type |
catalytic |
sequence |
I
|
description |
699
|
source |
MCSA : MCSA2
|
|
22)
|
chain |
B |
residue |
52 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
23)
|
chain |
B |
residue |
401 |
type |
BINDING |
sequence |
I
|
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
|
|
24)
|
chain |
B |
residue |
269 |
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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|
|