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Iron in PDB 1bvy: Complex of the Heme and Fmn-Binding Domains of the Cytochrome P450(Bm-3)

Enzymatic activity of Complex of the Heme and Fmn-Binding Domains of the Cytochrome P450(Bm-3)

All present enzymatic activity of Complex of the Heme and Fmn-Binding Domains of the Cytochrome P450(Bm-3):
1.14.14.1;

Protein crystallography data

The structure of Complex of the Heme and Fmn-Binding Domains of the Cytochrome P450(Bm-3), PDB code: 1bvy was solved by I.F.Sevrioukova, H.Li, H.Zhang, J.A.Peterson, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.03
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.840, 94.680, 209.060, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 27.5

Iron Binding Sites:

The binding sites of Iron atom in the Complex of the Heme and Fmn-Binding Domains of the Cytochrome P450(Bm-3) (pdb code 1bvy). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Complex of the Heme and Fmn-Binding Domains of the Cytochrome P450(Bm-3), PDB code: 1bvy:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1bvy

Go back to Iron Binding Sites List in 1bvy
Iron binding site 1 out of 2 in the Complex of the Heme and Fmn-Binding Domains of the Cytochrome P450(Bm-3)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Complex of the Heme and Fmn-Binding Domains of the Cytochrome P450(Bm-3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1000

b:18.1
occ:1.00
FE A:HEM1000 0.0 18.1 1.0
NA A:HEM1000 2.0 20.5 1.0
ND A:HEM1000 2.0 21.9 1.0
NB A:HEM1000 2.0 14.9 1.0
NC A:HEM1000 2.0 14.3 1.0
O1 A:EDO1003 2.1 18.9 1.0
SG A:CYS400 2.3 21.8 1.0
C1D A:HEM1000 3.0 18.7 1.0
C4C A:HEM1000 3.0 12.9 1.0
C1C A:HEM1000 3.0 14.7 1.0
C4A A:HEM1000 3.0 15.4 1.0
C4B A:HEM1000 3.0 10.5 1.0
C1A A:HEM1000 3.0 18.5 1.0
C4D A:HEM1000 3.0 13.5 1.0
C1B A:HEM1000 3.1 20.1 1.0
CB A:CYS400 3.2 19.9 1.0
C1 A:EDO1003 3.3 17.8 1.0
CHC A:HEM1000 3.4 12.6 1.0
CHD A:HEM1000 3.4 17.5 1.0
CHB A:HEM1000 3.4 21.2 1.0
CHA A:HEM1000 3.4 13.6 1.0
CA A:CYS400 4.1 16.6 1.0
C2 A:EDO1003 4.1 16.8 1.0
O A:ALA264 4.2 24.4 1.0
C2C A:HEM1000 4.3 11.8 1.0
C3C A:HEM1000 4.3 13.5 1.0
C3A A:HEM1000 4.3 12.8 1.0
C2A A:HEM1000 4.3 15.4 1.0
C3B A:HEM1000 4.3 13.0 1.0
C2D A:HEM1000 4.3 15.8 1.0
C3D A:HEM1000 4.3 17.6 1.0
C2B A:HEM1000 4.3 14.6 1.0
CB A:ALA264 4.6 9.6 1.0
C A:CYS400 4.8 20.9 1.0
N A:GLY402 4.8 17.4 1.0
C A:ALA264 4.8 13.8 1.0

Iron binding site 2 out of 2 in 1bvy

Go back to Iron Binding Sites List in 1bvy
Iron binding site 2 out of 2 in the Complex of the Heme and Fmn-Binding Domains of the Cytochrome P450(Bm-3)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Complex of the Heme and Fmn-Binding Domains of the Cytochrome P450(Bm-3) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1001

b:17.5
occ:1.00
FE B:HEM1001 0.0 17.5 1.0
ND B:HEM1001 2.0 13.8 1.0
NA B:HEM1001 2.0 17.1 1.0
NC B:HEM1001 2.0 12.6 1.0
NB B:HEM1001 2.0 11.6 1.0
O2 B:EDO1004 2.2 25.6 1.0
SG B:CYS400 2.3 20.8 1.0
C4A B:HEM1001 3.0 11.7 1.0
C1D B:HEM1001 3.0 19.5 1.0
C4D B:HEM1001 3.0 12.5 1.0
C1C B:HEM1001 3.0 13.1 1.0
C4C B:HEM1001 3.0 15.7 1.0
C1B B:HEM1001 3.0 14.5 1.0
C4B B:HEM1001 3.0 10.7 1.0
C1A B:HEM1001 3.1 13.1 1.0
CB B:CYS400 3.2 17.2 1.0
C2 B:EDO1004 3.3 25.8 1.0
CHB B:HEM1001 3.4 10.5 1.0
CHC B:HEM1001 3.4 9.6 1.0
CHD B:HEM1001 3.4 18.3 1.0
CHA B:HEM1001 3.4 10.2 1.0
CA B:CYS400 4.0 15.8 1.0
C1 B:EDO1004 4.1 22.9 1.0
O B:ALA264 4.2 18.6 1.0
C2D B:HEM1001 4.3 14.5 1.0
C3D B:HEM1001 4.3 12.4 1.0
C2C B:HEM1001 4.3 19.4 1.0
C3A B:HEM1001 4.3 9.9 1.0
C3B B:HEM1001 4.3 12.9 1.0
C3C B:HEM1001 4.3 17.4 1.0
C2B B:HEM1001 4.3 13.1 1.0
C2A B:HEM1001 4.3 13.0 1.0
CB B:ALA264 4.7 14.1 1.0
C B:CYS400 4.8 17.3 1.0
N B:GLY402 4.8 18.0 1.0
C B:ALA264 4.8 18.6 1.0

Reference:

I.F.Sevrioukova, H.Li, H.Zhang, J.A.Peterson, T.L.Poulos. Structure of A Cytochrome P450-Redox Partner Electron-Transfer Complex. Proc.Natl.Acad.Sci.Usa V. 96 1863 1999.
ISSN: ISSN 0027-8424
PubMed: 10051560
DOI: 10.1073/PNAS.96.5.1863
Page generated: Sat Aug 3 02:57:23 2024

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