Iron in PDB 2y5z: Mixed-Function P450 Mycg in Complex with Mycinamicin III in C2221 Space Group
Protein crystallography data
The structure of Mixed-Function P450 Mycg in Complex with Mycinamicin III in C2221 Space Group, PDB code: 2y5z
was solved by
S.Li,
P.M.Kells,
D.H.Sherman,
L.M.Podust,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
219.68 /
2.06
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
58.305,
100.882,
439.370,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
15 /
22.1
|
Iron Binding Sites:
The binding sites of Iron atom in the Mixed-Function P450 Mycg in Complex with Mycinamicin III in C2221 Space Group
(pdb code 2y5z). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the
Mixed-Function P450 Mycg in Complex with Mycinamicin III in C2221 Space Group, PDB code: 2y5z:
Jump to Iron binding site number:
1;
2;
3;
Iron binding site 1 out
of 3 in 2y5z
Go back to
Iron Binding Sites List in 2y5z
Iron binding site 1 out
of 3 in the Mixed-Function P450 Mycg in Complex with Mycinamicin III in C2221 Space Group
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Mixed-Function P450 Mycg in Complex with Mycinamicin III in C2221 Space Group within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe450
b:16.8
occ:1.00
|
FE
|
A:HEM450
|
0.0
|
16.8
|
1.0
|
NA
|
A:HEM450
|
1.9
|
15.7
|
1.0
|
NB
|
A:HEM450
|
2.0
|
14.1
|
1.0
|
NC
|
A:HEM450
|
2.0
|
14.5
|
1.0
|
ND
|
A:HEM450
|
2.1
|
14.8
|
1.0
|
SG
|
A:CYS346
|
2.4
|
16.3
|
1.0
|
O
|
A:HOH2162
|
2.4
|
18.5
|
1.0
|
C1A
|
A:HEM450
|
3.0
|
15.5
|
1.0
|
C4A
|
A:HEM450
|
3.0
|
16.4
|
1.0
|
C4B
|
A:HEM450
|
3.0
|
14.9
|
1.0
|
C1C
|
A:HEM450
|
3.0
|
15.1
|
1.0
|
C4D
|
A:HEM450
|
3.1
|
17.5
|
1.0
|
C4C
|
A:HEM450
|
3.1
|
15.5
|
1.0
|
C1B
|
A:HEM450
|
3.1
|
15.2
|
1.0
|
C1D
|
A:HEM450
|
3.1
|
15.8
|
1.0
|
CB
|
A:CYS346
|
3.4
|
14.3
|
1.0
|
CHA
|
A:HEM450
|
3.4
|
15.4
|
1.0
|
CHC
|
A:HEM450
|
3.4
|
12.6
|
1.0
|
CHB
|
A:HEM450
|
3.4
|
16.0
|
1.0
|
CHD
|
A:HEM450
|
3.5
|
14.9
|
1.0
|
CA
|
A:CYS346
|
4.0
|
15.7
|
1.0
|
C2A
|
A:HEM450
|
4.2
|
14.4
|
1.0
|
C3A
|
A:HEM450
|
4.2
|
16.4
|
1.0
|
O
|
A:ALA234
|
4.2
|
22.4
|
1.0
|
C2C
|
A:HEM450
|
4.3
|
16.8
|
1.0
|
C3B
|
A:HEM450
|
4.3
|
16.3
|
1.0
|
C3C
|
A:HEM450
|
4.3
|
18.0
|
1.0
|
C3D
|
A:HEM450
|
4.3
|
15.5
|
1.0
|
C2B
|
A:HEM450
|
4.3
|
16.6
|
1.0
|
C2D
|
A:HEM450
|
4.4
|
15.8
|
1.0
|
C
|
A:CYS346
|
4.7
|
17.3
|
1.0
|
N
|
A:GLY348
|
4.8
|
19.0
|
1.0
|
N
|
A:LEU347
|
4.8
|
18.4
|
1.0
|
|
Iron binding site 2 out
of 3 in 2y5z
Go back to
Iron Binding Sites List in 2y5z
Iron binding site 2 out
of 3 in the Mixed-Function P450 Mycg in Complex with Mycinamicin III in C2221 Space Group
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Mixed-Function P450 Mycg in Complex with Mycinamicin III in C2221 Space Group within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe450
b:17.2
occ:1.00
|
FE
|
B:HEM450
|
0.0
|
17.2
|
1.0
|
NB
|
B:HEM450
|
2.0
|
15.8
|
1.0
|
NC
|
B:HEM450
|
2.0
|
15.1
|
1.0
|
NA
|
B:HEM450
|
2.0
|
14.8
|
1.0
|
ND
|
B:HEM450
|
2.0
|
15.2
|
1.0
|
SG
|
B:CYS346
|
2.4
|
15.8
|
1.0
|
O
|
B:HOH2153
|
2.4
|
20.4
|
1.0
|
C4B
|
B:HEM450
|
3.0
|
15.1
|
1.0
|
C1C
|
B:HEM450
|
3.0
|
15.5
|
1.0
|
C4D
|
B:HEM450
|
3.0
|
16.4
|
1.0
|
C1A
|
B:HEM450
|
3.0
|
15.8
|
1.0
|
C4C
|
B:HEM450
|
3.1
|
15.8
|
1.0
|
C4A
|
B:HEM450
|
3.1
|
16.2
|
1.0
|
C1B
|
B:HEM450
|
3.1
|
17.0
|
1.0
|
C1D
|
B:HEM450
|
3.1
|
15.3
|
1.0
|
CB
|
B:CYS346
|
3.3
|
14.7
|
1.0
|
CHC
|
B:HEM450
|
3.4
|
13.2
|
1.0
|
CHA
|
B:HEM450
|
3.4
|
16.6
|
1.0
|
CHD
|
B:HEM450
|
3.5
|
14.8
|
1.0
|
CHB
|
B:HEM450
|
3.5
|
16.1
|
1.0
|
CA
|
B:CYS346
|
4.1
|
15.9
|
1.0
|
C3B
|
B:HEM450
|
4.2
|
17.0
|
1.0
|
C3C
|
B:HEM450
|
4.3
|
16.7
|
1.0
|
C2A
|
B:HEM450
|
4.3
|
15.0
|
1.0
|
C2C
|
B:HEM450
|
4.3
|
15.9
|
1.0
|
C3D
|
B:HEM450
|
4.3
|
15.9
|
1.0
|
O
|
B:ALA234
|
4.3
|
23.0
|
1.0
|
C3A
|
B:HEM450
|
4.3
|
15.6
|
1.0
|
C2B
|
B:HEM450
|
4.3
|
17.5
|
1.0
|
C2D
|
B:HEM450
|
4.3
|
14.8
|
1.0
|
C
|
B:CYS346
|
4.7
|
17.7
|
1.0
|
N
|
B:GLY348
|
4.8
|
19.2
|
1.0
|
N
|
B:LEU347
|
4.8
|
18.6
|
1.0
|
|
Iron binding site 3 out
of 3 in 2y5z
Go back to
Iron Binding Sites List in 2y5z
Iron binding site 3 out
of 3 in the Mixed-Function P450 Mycg in Complex with Mycinamicin III in C2221 Space Group
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Mixed-Function P450 Mycg in Complex with Mycinamicin III in C2221 Space Group within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe450
b:17.5
occ:1.00
|
FE
|
C:HEM450
|
0.0
|
17.5
|
1.0
|
NA
|
C:HEM450
|
2.0
|
15.5
|
1.0
|
ND
|
C:HEM450
|
2.1
|
15.5
|
1.0
|
NC
|
C:HEM450
|
2.1
|
14.9
|
1.0
|
NB
|
C:HEM450
|
2.1
|
16.6
|
1.0
|
SG
|
C:CYS346
|
2.3
|
16.3
|
1.0
|
O
|
C:HOH2149
|
2.5
|
22.2
|
1.0
|
C4A
|
C:HEM450
|
3.0
|
16.0
|
1.0
|
C1A
|
C:HEM450
|
3.0
|
16.1
|
1.0
|
C4B
|
C:HEM450
|
3.1
|
15.3
|
1.0
|
C4C
|
C:HEM450
|
3.1
|
16.0
|
1.0
|
C4D
|
C:HEM450
|
3.1
|
16.4
|
1.0
|
C1D
|
C:HEM450
|
3.1
|
16.2
|
1.0
|
C1C
|
C:HEM450
|
3.1
|
16.2
|
1.0
|
C1B
|
C:HEM450
|
3.1
|
16.2
|
1.0
|
CB
|
C:CYS346
|
3.4
|
13.8
|
1.0
|
CHA
|
C:HEM450
|
3.4
|
16.0
|
1.0
|
CHD
|
C:HEM450
|
3.4
|
15.4
|
1.0
|
CHC
|
C:HEM450
|
3.4
|
14.7
|
1.0
|
CHB
|
C:HEM450
|
3.5
|
16.4
|
1.0
|
CA
|
C:CYS346
|
4.0
|
15.1
|
1.0
|
C3A
|
C:HEM450
|
4.3
|
15.9
|
1.0
|
C2A
|
C:HEM450
|
4.3
|
14.3
|
1.0
|
O
|
C:ALA234
|
4.3
|
22.3
|
1.0
|
C3B
|
C:HEM450
|
4.3
|
16.6
|
1.0
|
C3D
|
C:HEM450
|
4.3
|
15.9
|
1.0
|
C3C
|
C:HEM450
|
4.3
|
17.4
|
1.0
|
C2D
|
C:HEM450
|
4.3
|
15.4
|
1.0
|
C2C
|
C:HEM450
|
4.3
|
16.8
|
1.0
|
C2B
|
C:HEM450
|
4.3
|
17.6
|
1.0
|
C
|
C:CYS346
|
4.7
|
17.0
|
1.0
|
N
|
C:GLY348
|
4.8
|
18.3
|
1.0
|
N
|
C:LEU347
|
4.9
|
18.2
|
1.0
|
|
Reference:
S.Li,
D.R.Tietz,
F.U.Rutaganira,
P.M.Kells,
Y.Anzai,
F.Kato,
T.C.Pochapsky,
D.H.Sherman,
L.M.Podust.
Substrate Recognition By the Multifunctional Cytochrome P450 Mycg in Mycinamicin Hydroxylation and Epoxidation Reactions. J.Biol.Chem. V. 287 37880 2012.
ISSN: ISSN 0021-9258
PubMed: 22952225
DOI: 10.1074/JBC.M112.410340
Page generated: Sun Aug 4 05:07:16 2024
|