Iron in PDB 6zmb: Structure of the Native Trna-Monooxygenase Enzyme Miae
Protein crystallography data
The structure of Structure of the Native Trna-Monooxygenase Enzyme Miae, PDB code: 6zmb
was solved by
P.Carpentier,
M.Atta,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.75 /
1.70
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
116.797,
50.929,
76.258,
90.00,
91.00,
90.00
|
R / Rfree (%)
|
18.8 /
21.7
|
Other elements in 6zmb:
The structure of Structure of the Native Trna-Monooxygenase Enzyme Miae also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Structure of the Native Trna-Monooxygenase Enzyme Miae
(pdb code 6zmb). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Structure of the Native Trna-Monooxygenase Enzyme Miae, PDB code: 6zmb:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 6zmb
Go back to
Iron Binding Sites List in 6zmb
Iron binding site 1 out
of 4 in the Structure of the Native Trna-Monooxygenase Enzyme Miae
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 Native Trna-Monooxygenase Enzyme Miae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe301
b:31.3
occ:1.00
|
O3
|
B:TRS306
|
2.0
|
40.2
|
1.0
|
OE1
|
B:GLU69
|
2.0
|
27.1
|
1.0
|
OE1
|
B:GLU38
|
2.0
|
25.5
|
1.0
|
O
|
B:HOH451
|
2.2
|
39.3
|
1.0
|
O
|
B:HOH412
|
2.2
|
28.7
|
1.0
|
ND1
|
B:HIS72
|
2.5
|
30.2
|
1.0
|
CD
|
B:GLU38
|
3.0
|
32.2
|
1.0
|
CD
|
B:GLU69
|
3.1
|
37.9
|
1.0
|
C3
|
B:TRS306
|
3.1
|
36.4
|
1.0
|
FE
|
B:FE302
|
3.2
|
35.8
|
1.0
|
OE2
|
B:GLU38
|
3.2
|
30.2
|
1.0
|
CE1
|
B:HIS72
|
3.3
|
34.6
|
1.0
|
OE2
|
B:GLU69
|
3.5
|
30.5
|
1.0
|
CG
|
B:HIS72
|
3.6
|
23.3
|
1.0
|
OE1
|
B:GLU151
|
3.8
|
37.6
|
1.0
|
CB
|
B:HIS72
|
3.9
|
22.0
|
1.0
|
O2
|
B:TRS306
|
4.0
|
42.5
|
1.0
|
C
|
B:TRS306
|
4.2
|
38.7
|
1.0
|
N
|
B:TRS306
|
4.2
|
42.8
|
1.0
|
CD
|
B:GLU151
|
4.2
|
38.6
|
1.0
|
OE2
|
B:GLU151
|
4.3
|
42.6
|
1.0
|
CG
|
B:GLU38
|
4.4
|
25.1
|
1.0
|
CG
|
B:GLU69
|
4.4
|
25.1
|
1.0
|
CE1
|
B:HIS154
|
4.4
|
40.4
|
1.0
|
NE2
|
B:HIS72
|
4.5
|
32.2
|
1.0
|
CA
|
B:GLU69
|
4.5
|
22.5
|
1.0
|
ND1
|
B:HIS154
|
4.6
|
31.5
|
1.0
|
CB
|
B:GLU69
|
4.7
|
19.6
|
1.0
|
CD2
|
B:HIS72
|
4.7
|
28.0
|
1.0
|
OG
|
B:SER150
|
4.7
|
46.3
|
1.0
|
C2
|
B:TRS306
|
4.7
|
30.8
|
1.0
|
CB
|
B:GLU38
|
4.8
|
22.2
|
1.0
|
|
Iron binding site 2 out
of 4 in 6zmb
Go back to
Iron Binding Sites List in 6zmb
Iron binding site 2 out
of 4 in the Structure of the Native Trna-Monooxygenase Enzyme Miae
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 Native Trna-Monooxygenase Enzyme Miae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe302
b:35.8
occ:1.00
|
OE1
|
B:GLU122
|
2.2
|
38.2
|
1.0
|
OE2
|
B:GLU69
|
2.2
|
30.5
|
1.0
|
ND1
|
B:HIS154
|
2.3
|
31.5
|
1.0
|
O
|
B:HOH451
|
2.3
|
39.3
|
1.0
|
O3
|
B:TRS306
|
2.4
|
40.2
|
1.0
|
O2
|
B:TRS306
|
2.5
|
42.5
|
1.0
|
OE2
|
B:GLU151
|
2.6
|
42.6
|
1.0
|
CE1
|
B:HIS154
|
3.1
|
40.4
|
1.0
|
CD
|
B:GLU69
|
3.1
|
37.9
|
1.0
|
FE
|
B:FE301
|
3.2
|
31.3
|
1.0
|
OE1
|
B:GLU69
|
3.2
|
27.1
|
1.0
|
CD
|
B:GLU122
|
3.3
|
35.5
|
1.0
|
CG
|
B:HIS154
|
3.4
|
35.1
|
1.0
|
C3
|
B:TRS306
|
3.4
|
36.4
|
1.0
|
CD
|
B:GLU151
|
3.5
|
38.6
|
1.0
|
O
|
B:HOH419
|
3.6
|
36.7
|
1.0
|
OE2
|
B:GLU122
|
3.8
|
46.0
|
1.0
|
CB
|
B:HIS154
|
3.8
|
27.9
|
1.0
|
OE1
|
B:GLU151
|
3.9
|
37.6
|
1.0
|
C2
|
B:TRS306
|
3.9
|
30.8
|
1.0
|
NE2
|
B:HIS154
|
4.3
|
34.4
|
1.0
|
O
|
B:HOH412
|
4.3
|
28.7
|
1.0
|
C
|
B:TRS306
|
4.3
|
38.7
|
1.0
|
CD2
|
B:HIS154
|
4.4
|
31.6
|
1.0
|
CG
|
B:GLU122
|
4.5
|
25.6
|
1.0
|
CG
|
B:GLU69
|
4.5
|
25.1
|
1.0
|
CA
|
B:GLU151
|
4.5
|
29.2
|
1.0
|
CG
|
B:GLU151
|
4.6
|
36.3
|
1.0
|
OE1
|
B:GLU38
|
4.8
|
25.5
|
1.0
|
CD1
|
B:LEU65
|
4.9
|
36.3
|
1.0
|
CB
|
B:GLU151
|
5.0
|
32.2
|
1.0
|
OG
|
B:SER150
|
5.0
|
46.3
|
1.0
|
O
|
B:SER150
|
5.0
|
31.4
|
1.0
|
|
Iron binding site 3 out
of 4 in 6zmb
Go back to
Iron Binding Sites List in 6zmb
Iron binding site 3 out
of 4 in the Structure of the Native Trna-Monooxygenase Enzyme Miae
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Structure of the Native Trna-Monooxygenase Enzyme Miae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe301
b:29.1
occ:1.00
|
O
|
C:HOH439
|
2.0
|
29.0
|
1.0
|
OE1
|
C:GLU69
|
2.0
|
23.6
|
1.0
|
OE1
|
C:GLU38
|
2.1
|
25.8
|
1.0
|
O
|
C:HOH412
|
2.1
|
24.6
|
1.0
|
O1
|
C:TRS303
|
2.2
|
35.8
|
1.0
|
ND1
|
C:HIS72
|
2.4
|
25.6
|
1.0
|
CD
|
C:GLU38
|
3.1
|
28.8
|
1.0
|
CD
|
C:GLU69
|
3.1
|
33.8
|
1.0
|
C1
|
C:TRS303
|
3.2
|
31.9
|
1.0
|
CE1
|
C:HIS72
|
3.2
|
28.6
|
1.0
|
FE
|
C:FE302
|
3.2
|
31.9
|
1.0
|
OE2
|
C:GLU38
|
3.4
|
30.3
|
1.0
|
CG
|
C:HIS72
|
3.4
|
22.5
|
1.0
|
OE2
|
C:GLU69
|
3.5
|
28.8
|
1.0
|
CB
|
C:HIS72
|
3.8
|
22.5
|
1.0
|
OE1
|
C:GLU151
|
3.9
|
34.6
|
1.0
|
O3
|
C:TRS303
|
4.3
|
51.4
|
1.0
|
OE2
|
C:GLU151
|
4.3
|
35.4
|
1.0
|
CD
|
C:GLU151
|
4.3
|
32.3
|
1.0
|
NE2
|
C:HIS72
|
4.4
|
27.5
|
1.0
|
C
|
C:TRS303
|
4.4
|
47.3
|
1.0
|
CG
|
C:GLU69
|
4.4
|
22.3
|
1.0
|
CG
|
C:GLU38
|
4.5
|
26.2
|
1.0
|
CA
|
C:GLU69
|
4.5
|
24.0
|
1.0
|
N
|
C:TRS303
|
4.5
|
45.9
|
1.0
|
CD2
|
C:HIS72
|
4.5
|
27.9
|
1.0
|
CE1
|
C:HIS154
|
4.6
|
29.9
|
1.0
|
OG
|
C:SER150
|
4.6
|
40.3
|
1.0
|
CB
|
C:GLU69
|
4.6
|
22.4
|
1.0
|
ND1
|
C:HIS154
|
4.7
|
30.7
|
1.0
|
CB
|
C:GLU38
|
4.8
|
23.1
|
1.0
|
C3
|
C:TRS303
|
4.9
|
48.2
|
1.0
|
|
Iron binding site 4 out
of 4 in 6zmb
Go back to
Iron Binding Sites List in 6zmb
Iron binding site 4 out
of 4 in the Structure of the Native Trna-Monooxygenase Enzyme Miae
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Structure of the Native Trna-Monooxygenase Enzyme Miae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe302
b:31.9
occ:1.00
|
O
|
C:HOH439
|
2.1
|
29.0
|
1.0
|
OE1
|
C:GLU122
|
2.1
|
33.0
|
1.0
|
OE2
|
C:GLU69
|
2.2
|
28.8
|
1.0
|
OE2
|
C:GLU151
|
2.4
|
35.4
|
1.0
|
O1
|
C:TRS303
|
2.4
|
35.8
|
1.0
|
ND1
|
C:HIS154
|
2.4
|
30.7
|
1.0
|
O3
|
C:TRS303
|
2.7
|
51.4
|
1.0
|
CD
|
C:GLU69
|
3.1
|
33.8
|
1.0
|
CE1
|
C:HIS154
|
3.2
|
29.9
|
1.0
|
FE
|
C:FE301
|
3.2
|
29.1
|
1.0
|
OE1
|
C:GLU69
|
3.3
|
23.6
|
1.0
|
CD
|
C:GLU122
|
3.3
|
34.6
|
1.0
|
CD
|
C:GLU151
|
3.3
|
32.3
|
1.0
|
C1
|
C:TRS303
|
3.4
|
31.9
|
1.0
|
CG
|
C:HIS154
|
3.5
|
26.5
|
1.0
|
O
|
C:HOH414
|
3.6
|
36.7
|
1.0
|
OE1
|
C:GLU151
|
3.7
|
34.6
|
1.0
|
OE2
|
C:GLU122
|
3.8
|
44.6
|
1.0
|
CB
|
C:HIS154
|
4.0
|
25.3
|
1.0
|
C3
|
C:TRS303
|
4.0
|
48.2
|
1.0
|
O
|
C:HOH412
|
4.2
|
24.6
|
1.0
|
C
|
C:TRS303
|
4.4
|
47.3
|
1.0
|
NE2
|
C:HIS154
|
4.4
|
30.9
|
1.0
|
CG
|
C:GLU122
|
4.5
|
24.4
|
1.0
|
CG
|
C:GLU69
|
4.5
|
22.3
|
1.0
|
CG
|
C:GLU151
|
4.5
|
30.9
|
1.0
|
CA
|
C:GLU151
|
4.5
|
25.7
|
1.0
|
CD2
|
C:HIS154
|
4.6
|
28.2
|
1.0
|
N
|
C:GLU151
|
4.9
|
27.2
|
1.0
|
CB
|
C:GLU151
|
4.9
|
25.6
|
1.0
|
OE1
|
C:GLU38
|
4.9
|
25.8
|
1.0
|
OG
|
C:SER150
|
4.9
|
40.3
|
1.0
|
ND1
|
C:HIS72
|
5.0
|
25.6
|
1.0
|
|
Reference:
P.Carpentier,
C.Lepretre,
C.Basset,
T.Douki,
S.Torelli,
V.Duarte,
D.Hamdane,
M.Fontecave,
M.Atta.
Structural, Biochemical and Functional Analyses of Trna-Monooxygenase Enzyme Miae From Pseudomonas Putida Provide Insights Into Trna/Miae Interaction. Nucleic Acids Res. V. 48 9918 2020.
ISSN: ESSN 1362-4962
PubMed: 32785618
DOI: 10.1093/NAR/GKAA667
Page generated: Wed Aug 7 20:25:34 2024
|