Iron in PDB 8ukz: Structure of P450BLT From Micromonospora Sp. Mw-13 with E238A Mutation
Protein crystallography data
The structure of Structure of P450BLT From Micromonospora Sp. Mw-13 with E238A Mutation, PDB code: 8ukz
was solved by
M.H.Hansen,
M.J.Cryle,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.24 /
1.95
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
61.957,
94.48,
105.985,
90,
92.68,
90
|
R / Rfree (%)
|
20.5 /
22.3
|
Other elements in 8ukz:
The structure of Structure of P450BLT From Micromonospora Sp. Mw-13 with E238A Mutation also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Structure of P450BLT From Micromonospora Sp. Mw-13 with E238A Mutation
(pdb code 8ukz). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the
Structure of P450BLT From Micromonospora Sp. Mw-13 with E238A Mutation, PDB code: 8ukz:
Jump to Iron binding site number:
1;
2;
3;
Iron binding site 1 out
of 3 in 8ukz
Go back to
Iron Binding Sites List in 8ukz
Iron binding site 1 out
of 3 in the Structure of P450BLT From Micromonospora Sp. Mw-13 with E238A Mutation
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Structure of P450BLT From Micromonospora Sp. Mw-13 with E238A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe401
b:27.0
occ:1.00
|
FE
|
A:HEM401
|
0.0
|
27.0
|
1.0
|
NB
|
A:HEM401
|
2.0
|
27.5
|
1.0
|
NA
|
A:HEM401
|
2.0
|
29.5
|
1.0
|
NC
|
A:HEM401
|
2.0
|
27.7
|
1.0
|
ND
|
A:HEM401
|
2.1
|
28.5
|
1.0
|
SG
|
A:CYS344
|
2.3
|
28.2
|
1.0
|
O
|
A:HOH539
|
2.8
|
39.1
|
1.0
|
C4B
|
A:HEM401
|
3.0
|
30.5
|
1.0
|
C1B
|
A:HEM401
|
3.1
|
27.1
|
1.0
|
C1C
|
A:HEM401
|
3.1
|
31.8
|
1.0
|
C1A
|
A:HEM401
|
3.1
|
28.7
|
1.0
|
C4A
|
A:HEM401
|
3.1
|
30.6
|
1.0
|
C4D
|
A:HEM401
|
3.1
|
30.0
|
1.0
|
C4C
|
A:HEM401
|
3.1
|
29.2
|
1.0
|
C1D
|
A:HEM401
|
3.1
|
31.2
|
1.0
|
HB2
|
A:CYS344
|
3.2
|
34.5
|
1.0
|
CB
|
A:CYS344
|
3.3
|
28.7
|
1.0
|
CHC
|
A:HEM401
|
3.4
|
29.3
|
1.0
|
CHB
|
A:HEM401
|
3.4
|
31.1
|
1.0
|
CHA
|
A:HEM401
|
3.4
|
29.2
|
1.0
|
CHD
|
A:HEM401
|
3.5
|
31.4
|
1.0
|
HA
|
A:CYS344
|
3.6
|
34.6
|
1.0
|
H
|
A:GLY346
|
3.8
|
38.8
|
1.0
|
HB1
|
A:ALA235
|
3.9
|
46.2
|
1.0
|
CA
|
A:CYS344
|
4.0
|
28.7
|
1.0
|
HB3
|
A:CYS344
|
4.2
|
34.5
|
1.0
|
C3B
|
A:HEM401
|
4.2
|
29.3
|
1.0
|
C2B
|
A:HEM401
|
4.2
|
28.4
|
1.0
|
C2A
|
A:HEM401
|
4.3
|
30.9
|
1.0
|
C2C
|
A:HEM401
|
4.3
|
29.7
|
1.0
|
C3A
|
A:HEM401
|
4.3
|
27.9
|
1.0
|
C3C
|
A:HEM401
|
4.3
|
31.0
|
1.0
|
C3D
|
A:HEM401
|
4.3
|
32.2
|
1.0
|
C2D
|
A:HEM401
|
4.3
|
28.0
|
1.0
|
H
|
A:LEU345
|
4.4
|
35.4
|
1.0
|
HHC
|
A:HEM401
|
4.4
|
35.2
|
1.0
|
HHB
|
A:HEM401
|
4.4
|
37.5
|
1.0
|
HHA
|
A:HEM401
|
4.4
|
35.1
|
1.0
|
HHD
|
A:HEM401
|
4.5
|
37.8
|
1.0
|
HD1
|
A:PHE337
|
4.5
|
35.4
|
1.0
|
N
|
A:GLY346
|
4.7
|
32.2
|
1.0
|
N
|
A:LEU345
|
4.7
|
29.4
|
1.0
|
C
|
A:CYS344
|
4.7
|
29.7
|
1.0
|
CB
|
A:ALA235
|
4.8
|
38.5
|
1.0
|
HB3
|
A:ALA235
|
4.8
|
46.2
|
1.0
|
OG
|
A:SER239
|
4.8
|
37.4
|
1.0
|
HA3
|
A:GLY346
|
4.9
|
35.9
|
1.0
|
HB2
|
A:SER239
|
4.9
|
38.7
|
1.0
|
|
Iron binding site 2 out
of 3 in 8ukz
Go back to
Iron Binding Sites List in 8ukz
Iron binding site 2 out
of 3 in the Structure of P450BLT From Micromonospora Sp. Mw-13 with E238A Mutation
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Structure of P450BLT From Micromonospora Sp. Mw-13 with E238A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe401
b:30.2
occ:1.00
|
FE
|
B:HEM401
|
0.0
|
30.2
|
1.0
|
NC
|
B:HEM401
|
2.0
|
29.4
|
1.0
|
ND
|
B:HEM401
|
2.0
|
26.5
|
1.0
|
NA
|
B:HEM401
|
2.1
|
24.9
|
1.0
|
NB
|
B:HEM401
|
2.1
|
26.8
|
1.0
|
SG
|
B:CYS344
|
2.3
|
30.2
|
1.0
|
C1C
|
B:HEM401
|
3.0
|
31.5
|
1.0
|
C4B
|
B:HEM401
|
3.0
|
30.4
|
1.0
|
C4D
|
B:HEM401
|
3.1
|
28.8
|
1.0
|
C1D
|
B:HEM401
|
3.1
|
28.3
|
1.0
|
C4C
|
B:HEM401
|
3.1
|
28.9
|
1.0
|
C1A
|
B:HEM401
|
3.1
|
28.8
|
1.0
|
C1B
|
B:HEM401
|
3.1
|
29.4
|
1.0
|
C4A
|
B:HEM401
|
3.1
|
28.8
|
1.0
|
HB2
|
B:CYS344
|
3.2
|
31.1
|
1.0
|
CB
|
B:CYS344
|
3.3
|
25.8
|
1.0
|
CHC
|
B:HEM401
|
3.4
|
29.7
|
1.0
|
CHD
|
B:HEM401
|
3.4
|
28.4
|
1.0
|
CHA
|
B:HEM401
|
3.4
|
29.8
|
1.0
|
CHB
|
B:HEM401
|
3.5
|
31.9
|
1.0
|
HA
|
B:CYS344
|
3.6
|
37.4
|
1.0
|
HB1
|
B:ALA235
|
3.9
|
43.7
|
1.0
|
H
|
B:GLY346
|
3.9
|
36.6
|
1.0
|
CA
|
B:CYS344
|
4.0
|
31.1
|
1.0
|
HB3
|
B:CYS344
|
4.1
|
31.1
|
1.0
|
C2C
|
B:HEM401
|
4.3
|
29.2
|
1.0
|
C3B
|
B:HEM401
|
4.3
|
27.6
|
1.0
|
C3C
|
B:HEM401
|
4.3
|
31.1
|
1.0
|
C2D
|
B:HEM401
|
4.3
|
29.6
|
1.0
|
C3D
|
B:HEM401
|
4.3
|
27.0
|
1.0
|
C2B
|
B:HEM401
|
4.3
|
31.3
|
1.0
|
C2A
|
B:HEM401
|
4.3
|
26.7
|
1.0
|
C3A
|
B:HEM401
|
4.3
|
27.9
|
1.0
|
HD1
|
B:PHE337
|
4.4
|
37.1
|
1.0
|
HHA
|
B:HEM401
|
4.4
|
35.8
|
1.0
|
HHC
|
B:HEM401
|
4.4
|
35.7
|
1.0
|
HHD
|
B:HEM401
|
4.4
|
34.2
|
1.0
|
HHB
|
B:HEM401
|
4.4
|
38.4
|
1.0
|
H
|
B:LEU345
|
4.4
|
38.7
|
1.0
|
C
|
B:CYS344
|
4.7
|
28.5
|
1.0
|
N
|
B:GLY346
|
4.7
|
30.4
|
1.0
|
CB
|
B:ALA235
|
4.7
|
36.3
|
1.0
|
HB3
|
B:ALA235
|
4.7
|
43.7
|
1.0
|
N
|
B:LEU345
|
4.7
|
32.2
|
1.0
|
OG
|
B:SER239
|
4.9
|
38.2
|
1.0
|
HA3
|
B:GLY346
|
4.9
|
36.7
|
1.0
|
HB2
|
B:SER239
|
4.9
|
37.7
|
1.0
|
|
Iron binding site 3 out
of 3 in 8ukz
Go back to
Iron Binding Sites List in 8ukz
Iron binding site 3 out
of 3 in the Structure of P450BLT From Micromonospora Sp. Mw-13 with E238A Mutation
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Structure of P450BLT From Micromonospora Sp. Mw-13 with E238A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe401
b:33.9
occ:1.00
|
FE
|
C:HEM401
|
0.0
|
33.9
|
1.0
|
NC
|
C:HEM401
|
2.0
|
35.0
|
1.0
|
ND
|
C:HEM401
|
2.0
|
35.2
|
1.0
|
NB
|
C:HEM401
|
2.1
|
37.2
|
1.0
|
NA
|
C:HEM401
|
2.1
|
39.0
|
1.0
|
SG
|
C:CYS344
|
2.3
|
36.6
|
1.0
|
C4C
|
C:HEM401
|
3.0
|
36.3
|
1.0
|
C1D
|
C:HEM401
|
3.0
|
34.9
|
1.0
|
C1C
|
C:HEM401
|
3.0
|
34.9
|
1.0
|
C4D
|
C:HEM401
|
3.0
|
35.7
|
1.0
|
C4B
|
C:HEM401
|
3.1
|
37.1
|
1.0
|
C1B
|
C:HEM401
|
3.1
|
36.9
|
1.0
|
C1A
|
C:HEM401
|
3.1
|
39.0
|
1.0
|
C4A
|
C:HEM401
|
3.1
|
37.8
|
1.0
|
HB2
|
C:CYS344
|
3.3
|
46.9
|
1.0
|
CB
|
C:CYS344
|
3.4
|
39.0
|
1.0
|
CHD
|
C:HEM401
|
3.4
|
36.5
|
1.0
|
CHC
|
C:HEM401
|
3.4
|
36.8
|
1.0
|
CHA
|
C:HEM401
|
3.4
|
37.9
|
1.0
|
CHB
|
C:HEM401
|
3.4
|
39.9
|
1.0
|
HA
|
C:CYS344
|
3.6
|
48.6
|
1.0
|
H
|
C:GLY346
|
3.8
|
49.9
|
1.0
|
HB1
|
C:ALA235
|
4.0
|
61.7
|
1.0
|
CA
|
C:CYS344
|
4.0
|
40.4
|
1.0
|
HB3
|
C:CYS344
|
4.2
|
46.9
|
1.0
|
C2D
|
C:HEM401
|
4.3
|
32.4
|
1.0
|
C3D
|
C:HEM401
|
4.3
|
36.5
|
1.0
|
C3C
|
C:HEM401
|
4.3
|
35.2
|
1.0
|
C2C
|
C:HEM401
|
4.3
|
32.6
|
1.0
|
C3B
|
C:HEM401
|
4.3
|
39.9
|
1.0
|
C2B
|
C:HEM401
|
4.3
|
38.0
|
1.0
|
C2A
|
C:HEM401
|
4.3
|
40.5
|
1.0
|
C3A
|
C:HEM401
|
4.3
|
39.3
|
1.0
|
HD1
|
C:PHE337
|
4.3
|
43.0
|
1.0
|
H
|
C:LEU345
|
4.4
|
52.5
|
1.0
|
HHD
|
C:HEM401
|
4.4
|
43.9
|
1.0
|
HHC
|
C:HEM401
|
4.4
|
44.2
|
1.0
|
HHA
|
C:HEM401
|
4.4
|
45.6
|
1.0
|
HHB
|
C:HEM401
|
4.4
|
48.0
|
1.0
|
N
|
C:GLY346
|
4.6
|
41.5
|
1.0
|
N
|
C:LEU345
|
4.7
|
43.7
|
1.0
|
C
|
C:CYS344
|
4.7
|
41.2
|
1.0
|
HB3
|
C:ALA235
|
4.8
|
61.7
|
1.0
|
HA3
|
C:GLY346
|
4.8
|
49.1
|
1.0
|
CB
|
C:ALA235
|
4.8
|
51.4
|
1.0
|
|
Reference:
M.H.Hansen,
A.Keto,
M.Treisman,
V.M.Sasi,
L.Coe,
Y.Zhao,
L.Padva,
C.Hess,
V.Leichthammer,
D.L.Machell,
R.B.Schittenhelm,
C.J.Jackson,
J.Tailhades,
M.Crusemann,
J.J.De Voss,
E.H.Krenske,
M.J.Cryle.
Structural Insights Into A Side Chain Cross-Linking Biarylitide P450 From Ripp Biosynthesis Acs Catalysis 812 2024.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.3C05417
Page generated: Sat Aug 10 18:36:50 2024
|