Iron in PDB 6wgw: CYP101D1 D259E Hydroxycamphor Bound
Protein crystallography data
The structure of CYP101D1 D259E Hydroxycamphor Bound, PDB code: 6wgw
was solved by
J.A.Amaya,
T.L.Poulos,
D.Batabyal,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.36 /
1.73
|
Space group
|
P 64 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
152.426,
152.426,
196.400,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
18.9 /
21.2
|
Iron Binding Sites:
The binding sites of Iron atom in the CYP101D1 D259E Hydroxycamphor Bound
(pdb code 6wgw). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
CYP101D1 D259E Hydroxycamphor Bound, PDB code: 6wgw:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 6wgw
Go back to
Iron Binding Sites List in 6wgw
Iron binding site 1 out
of 2 in the CYP101D1 D259E Hydroxycamphor Bound
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of CYP101D1 D259E Hydroxycamphor Bound within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe501
b:17.3
occ:1.00
|
FE
|
A:HEM501
|
0.0
|
17.3
|
1.0
|
NA
|
A:HEM501
|
2.0
|
17.6
|
1.0
|
NC
|
A:HEM501
|
2.0
|
18.4
|
1.0
|
ND
|
A:HEM501
|
2.0
|
18.1
|
1.0
|
NB
|
A:HEM501
|
2.0
|
16.8
|
1.0
|
SG
|
A:CYS365
|
2.4
|
20.9
|
1.0
|
O5
|
A:CAH502
|
2.7
|
27.4
|
0.6
|
C1C
|
A:HEM501
|
3.0
|
19.7
|
1.0
|
C4A
|
A:HEM501
|
3.0
|
17.8
|
1.0
|
C4B
|
A:HEM501
|
3.0
|
18.3
|
1.0
|
C1A
|
A:HEM501
|
3.0
|
19.6
|
1.0
|
C1D
|
A:HEM501
|
3.0
|
20.7
|
1.0
|
C4D
|
A:HEM501
|
3.1
|
17.4
|
1.0
|
C1B
|
A:HEM501
|
3.1
|
17.2
|
1.0
|
C4C
|
A:HEM501
|
3.1
|
18.5
|
1.0
|
CHC
|
A:HEM501
|
3.4
|
19.6
|
1.0
|
CB
|
A:CYS365
|
3.4
|
18.5
|
1.0
|
CHB
|
A:HEM501
|
3.4
|
15.3
|
1.0
|
CHA
|
A:HEM501
|
3.4
|
17.6
|
1.0
|
CHD
|
A:HEM501
|
3.4
|
20.3
|
1.0
|
C5
|
A:CAH502
|
3.9
|
30.0
|
0.6
|
CA
|
A:CYS365
|
4.1
|
17.1
|
1.0
|
C2C
|
A:HEM501
|
4.2
|
22.2
|
1.0
|
C3A
|
A:HEM501
|
4.2
|
17.8
|
1.0
|
C2A
|
A:HEM501
|
4.3
|
17.9
|
1.0
|
C2D
|
A:HEM501
|
4.3
|
20.7
|
1.0
|
C3B
|
A:HEM501
|
4.3
|
16.9
|
1.0
|
C3C
|
A:HEM501
|
4.3
|
20.5
|
1.0
|
C3D
|
A:HEM501
|
4.3
|
20.6
|
1.0
|
C2B
|
A:HEM501
|
4.3
|
17.6
|
1.0
|
N
|
A:GLY367
|
4.5
|
18.6
|
1.0
|
C4
|
A:CAH502
|
4.5
|
30.1
|
0.6
|
C
|
A:CYS365
|
4.7
|
19.6
|
1.0
|
N
|
A:ALA366
|
4.7
|
19.5
|
1.0
|
CA
|
A:GLY367
|
4.8
|
19.4
|
1.0
|
CG2
|
A:THR260
|
4.9
|
30.1
|
0.5
|
|
Iron binding site 2 out
of 2 in 6wgw
Go back to
Iron Binding Sites List in 6wgw
Iron binding site 2 out
of 2 in the CYP101D1 D259E Hydroxycamphor Bound
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of CYP101D1 D259E Hydroxycamphor Bound within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe501
b:19.0
occ:1.00
|
FE
|
B:HEM501
|
0.0
|
19.0
|
1.0
|
ND
|
B:HEM501
|
2.0
|
19.5
|
1.0
|
NA
|
B:HEM501
|
2.0
|
16.0
|
1.0
|
NB
|
B:HEM501
|
2.0
|
17.8
|
1.0
|
NC
|
B:HEM501
|
2.1
|
16.7
|
1.0
|
SG
|
B:CYS365
|
2.5
|
21.0
|
1.0
|
O5
|
B:CAH502
|
2.9
|
28.8
|
0.3
|
C1D
|
B:HEM501
|
3.0
|
21.1
|
1.0
|
C4A
|
B:HEM501
|
3.0
|
18.5
|
1.0
|
C4D
|
B:HEM501
|
3.1
|
19.5
|
1.0
|
C1B
|
B:HEM501
|
3.1
|
19.6
|
1.0
|
C4B
|
B:HEM501
|
3.1
|
18.8
|
1.0
|
C1A
|
B:HEM501
|
3.1
|
18.0
|
1.0
|
C1C
|
B:HEM501
|
3.1
|
20.2
|
1.0
|
C4C
|
B:HEM501
|
3.1
|
20.7
|
1.0
|
CB
|
B:CYS365
|
3.3
|
18.2
|
1.0
|
CHD
|
B:HEM501
|
3.4
|
20.5
|
1.0
|
CHB
|
B:HEM501
|
3.4
|
17.3
|
1.0
|
CHA
|
B:HEM501
|
3.5
|
18.1
|
1.0
|
CHC
|
B:HEM501
|
3.5
|
21.7
|
1.0
|
CA
|
B:CYS365
|
4.0
|
15.8
|
1.0
|
C5
|
B:CAH502
|
4.1
|
29.1
|
0.3
|
C5
|
B:CAM503
|
4.1
|
29.1
|
0.5
|
C2D
|
B:HEM501
|
4.2
|
19.9
|
1.0
|
C3D
|
B:HEM501
|
4.3
|
18.6
|
1.0
|
C3A
|
B:HEM501
|
4.3
|
16.4
|
1.0
|
C2B
|
B:HEM501
|
4.3
|
18.1
|
1.0
|
C3B
|
B:HEM501
|
4.3
|
18.8
|
1.0
|
C2A
|
B:HEM501
|
4.3
|
16.4
|
1.0
|
C2C
|
B:HEM501
|
4.3
|
20.7
|
1.0
|
C3C
|
B:HEM501
|
4.3
|
20.0
|
1.0
|
N
|
B:GLY367
|
4.4
|
19.8
|
1.0
|
C
|
B:CYS365
|
4.6
|
19.0
|
1.0
|
C4
|
B:CAH502
|
4.6
|
28.9
|
0.3
|
N
|
B:ALA366
|
4.6
|
18.9
|
1.0
|
C8
|
B:CAM503
|
4.6
|
27.9
|
0.5
|
C4
|
B:CAM503
|
4.7
|
28.8
|
0.5
|
CA
|
B:GLY367
|
4.8
|
18.0
|
1.0
|
CG2
|
B:THR260
|
4.8
|
29.1
|
1.0
|
C9
|
B:CAH502
|
5.0
|
28.0
|
0.3
|
|
Reference:
J.A.Amaya,
D.Batabyal,
T.L.Poulos.
Proton Relay Network in the Bacterial P450S: CYP101A1 and CYP101D1. Biochemistry V. 59 2896 2020.
ISSN: ISSN 0006-2960
PubMed: 32574066
DOI: 10.1021/ACS.BIOCHEM.0C00329
Page generated: Wed Aug 7 14:00:47 2024
|