Iron in PDB 4kf2: Structure of the P4509 BM3 A82F F87V Heme Domain
Enzymatic activity of Structure of the P4509 BM3 A82F F87V Heme Domain
All present enzymatic activity of Structure of the P4509 BM3 A82F F87V Heme Domain:
1.14.14.1;
1.6.2.4;
Protein crystallography data
The structure of Structure of the P4509 BM3 A82F F87V Heme Domain, PDB code: 4kf2
was solved by
D.Leys,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.00 /
1.82
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
59.270,
151.670,
60.800,
90.00,
95.89,
90.00
|
R / Rfree (%)
|
18.3 /
22.5
|
Iron Binding Sites:
The binding sites of Iron atom in the Structure of the P4509 BM3 A82F F87V Heme Domain
(pdb code 4kf2). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Structure of the P4509 BM3 A82F F87V Heme Domain, PDB code: 4kf2:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 4kf2
Go back to
Iron Binding Sites List in 4kf2
Iron binding site 1 out
of 2 in the Structure of the P4509 BM3 A82F F87V Heme Domain
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Structure of the P4509 BM3 A82F F87V Heme Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe501
b:19.8
occ:1.00
|
FE
|
A:HEM501
|
0.0
|
19.8
|
1.0
|
N1
|
A:IMD502
|
1.8
|
18.1
|
1.0
|
NA
|
A:HEM501
|
2.0
|
18.7
|
1.0
|
NC
|
A:HEM501
|
2.0
|
19.9
|
1.0
|
NB
|
A:HEM501
|
2.1
|
14.8
|
1.0
|
ND
|
A:HEM501
|
2.1
|
15.4
|
1.0
|
SG
|
A:CYS400
|
2.2
|
21.4
|
1.0
|
C2
|
A:IMD502
|
2.8
|
21.4
|
1.0
|
C1D
|
A:HEM501
|
3.0
|
20.4
|
1.0
|
C4B
|
A:HEM501
|
3.0
|
16.8
|
1.0
|
C5
|
A:IMD502
|
3.0
|
23.0
|
1.0
|
C1B
|
A:HEM501
|
3.0
|
18.5
|
1.0
|
C4A
|
A:HEM501
|
3.1
|
16.7
|
1.0
|
C4C
|
A:HEM501
|
3.1
|
22.0
|
1.0
|
C1A
|
A:HEM501
|
3.1
|
14.8
|
1.0
|
C1C
|
A:HEM501
|
3.1
|
19.5
|
1.0
|
C4D
|
A:HEM501
|
3.1
|
20.4
|
1.0
|
CHD
|
A:HEM501
|
3.3
|
21.8
|
1.0
|
CB
|
A:CYS400
|
3.4
|
19.0
|
1.0
|
CHB
|
A:HEM501
|
3.4
|
17.0
|
1.0
|
CHC
|
A:HEM501
|
3.4
|
18.9
|
1.0
|
CHA
|
A:HEM501
|
3.5
|
19.8
|
1.0
|
N3
|
A:IMD502
|
4.0
|
25.0
|
1.0
|
CA
|
A:CYS400
|
4.1
|
19.0
|
1.0
|
C4
|
A:IMD502
|
4.2
|
25.1
|
1.0
|
C3B
|
A:HEM501
|
4.2
|
13.5
|
1.0
|
C2B
|
A:HEM501
|
4.3
|
17.4
|
1.0
|
C2D
|
A:HEM501
|
4.3
|
16.7
|
1.0
|
C3A
|
A:HEM501
|
4.3
|
19.5
|
1.0
|
C3C
|
A:HEM501
|
4.3
|
22.3
|
1.0
|
C2A
|
A:HEM501
|
4.3
|
20.4
|
1.0
|
C2C
|
A:HEM501
|
4.3
|
19.9
|
1.0
|
C3D
|
A:HEM501
|
4.3
|
17.5
|
1.0
|
C
|
A:CYS400
|
4.8
|
18.6
|
1.0
|
N
|
A:GLY402
|
4.8
|
23.8
|
1.0
|
N
|
A:ILE401
|
4.9
|
20.5
|
1.0
|
|
Iron binding site 2 out
of 2 in 4kf2
Go back to
Iron Binding Sites List in 4kf2
Iron binding site 2 out
of 2 in the Structure of the P4509 BM3 A82F F87V Heme Domain
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Structure of the P4509 BM3 A82F F87V Heme Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe501
b:17.1
occ:1.00
|
FE
|
B:HEM501
|
0.0
|
17.1
|
1.0
|
ND
|
B:HEM501
|
2.0
|
13.2
|
1.0
|
NA
|
B:HEM501
|
2.0
|
18.0
|
1.0
|
NB
|
B:HEM501
|
2.0
|
12.6
|
1.0
|
NC
|
B:HEM501
|
2.0
|
18.6
|
1.0
|
N1
|
B:IMD502
|
2.1
|
17.7
|
1.0
|
SG
|
B:CYS400
|
2.2
|
17.1
|
1.0
|
C1D
|
B:HEM501
|
2.9
|
16.8
|
1.0
|
C1B
|
B:HEM501
|
2.9
|
17.6
|
1.0
|
C4C
|
B:HEM501
|
3.0
|
16.2
|
1.0
|
C2
|
B:IMD502
|
3.0
|
21.8
|
1.0
|
C4A
|
B:HEM501
|
3.0
|
16.6
|
1.0
|
C4D
|
B:HEM501
|
3.1
|
13.7
|
1.0
|
C4B
|
B:HEM501
|
3.1
|
15.1
|
1.0
|
C1A
|
B:HEM501
|
3.1
|
16.1
|
1.0
|
C1C
|
B:HEM501
|
3.1
|
13.4
|
1.0
|
C5
|
B:IMD502
|
3.2
|
22.3
|
1.0
|
CHD
|
B:HEM501
|
3.3
|
17.5
|
1.0
|
CB
|
B:CYS400
|
3.3
|
17.4
|
1.0
|
CHB
|
B:HEM501
|
3.3
|
19.2
|
1.0
|
CHA
|
B:HEM501
|
3.4
|
15.1
|
1.0
|
CHC
|
B:HEM501
|
3.5
|
14.0
|
1.0
|
CA
|
B:CYS400
|
4.1
|
18.0
|
1.0
|
N3
|
B:IMD502
|
4.2
|
20.5
|
1.0
|
C2D
|
B:HEM501
|
4.2
|
13.2
|
1.0
|
C2B
|
B:HEM501
|
4.2
|
14.3
|
1.0
|
C3B
|
B:HEM501
|
4.2
|
14.8
|
1.0
|
C3C
|
B:HEM501
|
4.2
|
16.3
|
1.0
|
C3D
|
B:HEM501
|
4.3
|
13.2
|
1.0
|
C3A
|
B:HEM501
|
4.3
|
18.6
|
1.0
|
C2C
|
B:HEM501
|
4.3
|
16.7
|
1.0
|
C2A
|
B:HEM501
|
4.3
|
17.9
|
1.0
|
C4
|
B:IMD502
|
4.3
|
19.8
|
1.0
|
C
|
B:CYS400
|
4.8
|
16.1
|
1.0
|
N
|
B:GLY402
|
4.9
|
18.9
|
1.0
|
N
|
B:ILE401
|
5.0
|
17.1
|
1.0
|
|
Reference:
C.F.Butler,
C.Peet,
A.E.Mason,
M.W.Voice,
D.Leys,
A.W.Munro.
Key Mutations Alter the Cytochrome P450 BM3 Conformational Landscape and Remove Inherent Substrate Bias. J.Biol.Chem. V. 288 25387 2013.
ISSN: ISSN 0021-9258
PubMed: 23828198
DOI: 10.1074/JBC.M113.479717
Page generated: Sun Dec 13 15:39:45 2020
|