Iron in PDB 1sqp: Crystal Structure Analysis of Bovine BC1 with Myxothiazol
Enzymatic activity of Crystal Structure Analysis of Bovine BC1 with Myxothiazol
All present enzymatic activity of Crystal Structure Analysis of Bovine BC1 with Myxothiazol:
1.10.2.2;
Protein crystallography data
The structure of Crystal Structure Analysis of Bovine BC1 with Myxothiazol, PDB code: 1sqp
was solved by
L.Esser,
B.Quinn,
Y.F.Li,
M.Zhang,
M.Elberry,
L.Yu,
C.A.Yu,
D.Xia,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.00 /
2.70
|
Space group
|
I 41 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
153.700,
153.700,
596.534,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
26.3 /
31.4
|
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure Analysis of Bovine BC1 with Myxothiazol
(pdb code 1sqp). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 5 binding sites of Iron where determined in the
Crystal Structure Analysis of Bovine BC1 with Myxothiazol, PDB code: 1sqp:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
Iron binding site 1 out
of 5 in 1sqp
Go back to
Iron Binding Sites List in 1sqp
Iron binding site 1 out
of 5 in the Crystal Structure Analysis of Bovine BC1 with Myxothiazol
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure Analysis of Bovine BC1 with Myxothiazol within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe381
b:62.3
occ:1.00
|
FE
|
C:HEM381
|
0.0
|
62.3
|
1.0
|
NC
|
C:HEM381
|
2.0
|
64.7
|
1.0
|
ND
|
C:HEM381
|
2.0
|
63.2
|
1.0
|
NB
|
C:HEM381
|
2.0
|
66.9
|
1.0
|
NA
|
C:HEM381
|
2.0
|
61.6
|
1.0
|
NE2
|
C:HIS196
|
2.2
|
10.5
|
1.0
|
NE2
|
C:HIS97
|
2.2
|
19.4
|
1.0
|
C4A
|
C:HEM381
|
3.0
|
62.4
|
1.0
|
C1C
|
C:HEM381
|
3.0
|
68.4
|
1.0
|
C4C
|
C:HEM381
|
3.0
|
64.6
|
1.0
|
C1A
|
C:HEM381
|
3.0
|
62.3
|
1.0
|
C1D
|
C:HEM381
|
3.0
|
65.0
|
1.0
|
C4B
|
C:HEM381
|
3.0
|
69.7
|
1.0
|
C1B
|
C:HEM381
|
3.0
|
66.5
|
1.0
|
C4D
|
C:HEM381
|
3.0
|
62.1
|
1.0
|
CD2
|
C:HIS196
|
3.1
|
15.0
|
1.0
|
CD2
|
C:HIS97
|
3.1
|
17.2
|
1.0
|
CE1
|
C:HIS196
|
3.1
|
13.7
|
1.0
|
CE1
|
C:HIS97
|
3.3
|
18.3
|
1.0
|
CHB
|
C:HEM381
|
3.4
|
63.6
|
1.0
|
CHC
|
C:HEM381
|
3.4
|
70.2
|
1.0
|
CHA
|
C:HEM381
|
3.5
|
63.7
|
1.0
|
CHD
|
C:HEM381
|
3.5
|
63.9
|
1.0
|
C3A
|
C:HEM381
|
4.2
|
61.5
|
1.0
|
C2C
|
C:HEM381
|
4.2
|
68.9
|
1.0
|
C2A
|
C:HEM381
|
4.2
|
60.0
|
1.0
|
ND1
|
C:HIS196
|
4.2
|
13.7
|
1.0
|
CG
|
C:HIS196
|
4.2
|
16.1
|
1.0
|
C3D
|
C:HEM381
|
4.2
|
61.7
|
1.0
|
C2D
|
C:HEM381
|
4.2
|
63.8
|
1.0
|
C3C
|
C:HEM381
|
4.2
|
67.6
|
1.0
|
C3B
|
C:HEM381
|
4.3
|
72.2
|
1.0
|
C2B
|
C:HEM381
|
4.3
|
69.9
|
1.0
|
CG
|
C:HIS97
|
4.3
|
14.8
|
1.0
|
ND1
|
C:HIS97
|
4.4
|
21.6
|
1.0
|
CD1
|
C:LEU37
|
4.9
|
8.9
|
1.0
|
|
Iron binding site 2 out
of 5 in 1sqp
Go back to
Iron Binding Sites List in 1sqp
Iron binding site 2 out
of 5 in the Crystal Structure Analysis of Bovine BC1 with Myxothiazol
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure Analysis of Bovine BC1 with Myxothiazol within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe382
b:88.9
occ:1.00
|
FE
|
C:HEM382
|
0.0
|
88.9
|
1.0
|
ND
|
C:HEM382
|
2.0
|
94.8
|
1.0
|
NC
|
C:HEM382
|
2.0
|
97.8
|
1.0
|
NB
|
C:HEM382
|
2.0
|
97.0
|
1.0
|
NA
|
C:HEM382
|
2.0
|
96.5
|
1.0
|
NE2
|
C:HIS83
|
2.1
|
3.0
|
1.0
|
NE2
|
C:HIS182
|
2.2
|
2.0
|
1.0
|
C1A
|
C:HEM382
|
3.0
|
96.2
|
1.0
|
C4D
|
C:HEM382
|
3.0
|
94.1
|
1.0
|
C4A
|
C:HEM382
|
3.0
|
97.2
|
1.0
|
CE1
|
C:HIS83
|
3.0
|
8.9
|
1.0
|
C1C
|
C:HEM382
|
3.0
|
98.0
|
1.0
|
C4C
|
C:HEM382
|
3.1
|
97.4
|
1.0
|
C4B
|
C:HEM382
|
3.1
|
96.3
|
1.0
|
C1D
|
C:HEM382
|
3.1
|
94.3
|
1.0
|
C1B
|
C:HEM382
|
3.1
|
97.3
|
1.0
|
CD2
|
C:HIS83
|
3.1
|
6.5
|
1.0
|
CD2
|
C:HIS182
|
3.2
|
10.4
|
1.0
|
CE1
|
C:HIS182
|
3.2
|
8.2
|
1.0
|
CHA
|
C:HEM382
|
3.4
|
95.6
|
1.0
|
CHC
|
C:HEM382
|
3.5
|
97.6
|
1.0
|
CHB
|
C:HEM382
|
3.5
|
98.0
|
1.0
|
CHD
|
C:HEM382
|
3.5
|
96.5
|
1.0
|
ND1
|
C:HIS83
|
4.2
|
12.3
|
1.0
|
C3D
|
C:HEM382
|
4.3
|
91.6
|
1.0
|
C2A
|
C:HEM382
|
4.3
|
97.6
|
1.0
|
CG
|
C:HIS83
|
4.3
|
9.5
|
1.0
|
ND1
|
C:HIS182
|
4.3
|
11.7
|
1.0
|
C3A
|
C:HEM382
|
4.3
|
97.5
|
1.0
|
C2D
|
C:HEM382
|
4.3
|
92.4
|
1.0
|
C2C
|
C:HEM382
|
4.3
|
98.0
|
1.0
|
CG
|
C:HIS182
|
4.3
|
14.3
|
1.0
|
C3C
|
C:HEM382
|
4.3
|
98.2
|
1.0
|
C2B
|
C:HEM382
|
4.3
|
96.6
|
1.0
|
C3B
|
C:HEM382
|
4.3
|
95.9
|
1.0
|
OE1
|
C:GLN44
|
5.0
|
26.4
|
1.0
|
|
Iron binding site 3 out
of 5 in 1sqp
Go back to
Iron Binding Sites List in 1sqp
Iron binding site 3 out
of 5 in the Crystal Structure Analysis of Bovine BC1 with Myxothiazol
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure Analysis of Bovine BC1 with Myxothiazol within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe243
b:85.9
occ:1.00
|
FE
|
D:HEM243
|
0.0
|
85.9
|
1.0
|
NC
|
D:HEM243
|
2.0
|
86.1
|
1.0
|
ND
|
D:HEM243
|
2.0
|
83.5
|
1.0
|
NB
|
D:HEM243
|
2.0
|
82.5
|
1.0
|
NA
|
D:HEM243
|
2.0
|
85.0
|
1.0
|
NE2
|
D:HIS41
|
2.3
|
22.1
|
1.0
|
SD
|
D:MET160
|
2.5
|
27.7
|
1.0
|
C1A
|
D:HEM243
|
3.0
|
86.0
|
1.0
|
C4C
|
D:HEM243
|
3.0
|
88.2
|
1.0
|
C4A
|
D:HEM243
|
3.0
|
83.5
|
1.0
|
C1C
|
D:HEM243
|
3.0
|
87.1
|
1.0
|
C1D
|
D:HEM243
|
3.0
|
85.9
|
1.0
|
C1B
|
D:HEM243
|
3.1
|
81.8
|
1.0
|
C4B
|
D:HEM243
|
3.1
|
83.6
|
1.0
|
C4D
|
D:HEM243
|
3.1
|
85.9
|
1.0
|
CD2
|
D:HIS41
|
3.1
|
22.4
|
1.0
|
CE1
|
D:HIS41
|
3.4
|
21.4
|
1.0
|
CHA
|
D:HEM243
|
3.5
|
86.3
|
1.0
|
CHD
|
D:HEM243
|
3.5
|
88.0
|
1.0
|
CHC
|
D:HEM243
|
3.5
|
87.0
|
1.0
|
CHB
|
D:HEM243
|
3.5
|
82.0
|
1.0
|
CG
|
D:MET160
|
3.6
|
28.9
|
1.0
|
CE
|
D:MET160
|
4.1
|
29.1
|
1.0
|
C2A
|
D:HEM243
|
4.2
|
86.3
|
1.0
|
C3A
|
D:HEM243
|
4.2
|
83.9
|
1.0
|
C2C
|
D:HEM243
|
4.3
|
86.6
|
1.0
|
C3D
|
D:HEM243
|
4.3
|
87.5
|
1.0
|
C3C
|
D:HEM243
|
4.3
|
89.0
|
1.0
|
C2D
|
D:HEM243
|
4.3
|
87.0
|
1.0
|
C2B
|
D:HEM243
|
4.3
|
81.5
|
1.0
|
CG
|
D:HIS41
|
4.3
|
24.4
|
1.0
|
C3B
|
D:HEM243
|
4.3
|
82.5
|
1.0
|
ND1
|
D:HIS41
|
4.4
|
22.5
|
1.0
|
CB
|
D:MET160
|
4.6
|
29.8
|
1.0
|
|
Iron binding site 4 out
of 5 in 1sqp
Go back to
Iron Binding Sites List in 1sqp
Iron binding site 4 out
of 5 in the Crystal Structure Analysis of Bovine BC1 with Myxothiazol
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure Analysis of Bovine BC1 with Myxothiazol within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe198
b:0.0
occ:1.00
|
FE1
|
E:FES198
|
0.0
|
0.0
|
1.0
|
S1
|
E:FES198
|
2.2
|
0.2
|
1.0
|
S2
|
E:FES198
|
2.2
|
0.8
|
1.0
|
SG
|
E:CYS158
|
2.6
|
31.8
|
1.0
|
FE2
|
E:FES198
|
2.8
|
0.9
|
1.0
|
SG
|
E:CYS139
|
3.2
|
28.1
|
1.0
|
CB
|
E:CYS158
|
3.3
|
30.0
|
1.0
|
CB
|
E:CYS139
|
3.4
|
29.2
|
1.0
|
CB
|
E:CYS144
|
4.0
|
27.5
|
1.0
|
CB
|
E:CYS160
|
4.2
|
27.7
|
1.0
|
CB
|
E:SER163
|
4.6
|
29.4
|
1.0
|
SG
|
E:CYS144
|
4.6
|
25.8
|
1.0
|
N
|
E:CYS144
|
4.6
|
27.9
|
1.0
|
CA
|
E:CYS158
|
4.7
|
30.2
|
1.0
|
CA
|
E:CYS144
|
4.7
|
27.8
|
1.0
|
O
|
E:CYS144
|
4.7
|
28.5
|
1.0
|
OH
|
E:TYR165
|
4.8
|
22.3
|
1.0
|
C
|
E:CYS144
|
4.9
|
28.4
|
1.0
|
N
|
E:HIS161
|
4.9
|
28.7
|
1.0
|
OG
|
E:SER163
|
4.9
|
28.9
|
1.0
|
CA
|
E:CYS139
|
4.9
|
29.6
|
1.0
|
|
Iron binding site 5 out
of 5 in 1sqp
Go back to
Iron Binding Sites List in 1sqp
Iron binding site 5 out
of 5 in the Crystal Structure Analysis of Bovine BC1 with Myxothiazol
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Crystal Structure Analysis of Bovine BC1 with Myxothiazol within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe198
b:0.9
occ:1.00
|
FE2
|
E:FES198
|
0.0
|
0.9
|
1.0
|
S2
|
E:FES198
|
2.2
|
0.8
|
1.0
|
S1
|
E:FES198
|
2.2
|
0.2
|
1.0
|
FE1
|
E:FES198
|
2.8
|
0.0
|
1.0
|
ND1
|
E:HIS161
|
2.9
|
30.3
|
1.0
|
CB
|
E:CYS160
|
3.3
|
27.7
|
1.0
|
N
|
E:HIS161
|
3.4
|
28.7
|
1.0
|
ND1
|
E:HIS141
|
3.6
|
30.9
|
1.0
|
CG
|
E:HIS161
|
3.6
|
29.6
|
1.0
|
CB
|
E:HIS161
|
3.7
|
29.0
|
1.0
|
CE1
|
E:HIS161
|
3.8
|
30.5
|
1.0
|
CB
|
E:LEU142
|
3.9
|
29.6
|
1.0
|
CA
|
E:HIS161
|
4.1
|
29.0
|
1.0
|
CE1
|
E:HIS141
|
4.2
|
31.6
|
1.0
|
SG
|
E:CYS144
|
4.2
|
25.8
|
1.0
|
C
|
E:CYS160
|
4.4
|
28.2
|
1.0
|
CA
|
E:CYS160
|
4.4
|
28.0
|
1.0
|
SG
|
E:CYS160
|
4.4
|
25.8
|
1.0
|
CB
|
E:CYS144
|
4.8
|
27.5
|
1.0
|
CG
|
E:HIS141
|
4.8
|
30.7
|
1.0
|
CD2
|
E:HIS161
|
4.8
|
29.8
|
1.0
|
N
|
E:LEU142
|
4.8
|
30.0
|
1.0
|
CG
|
E:LEU142
|
4.8
|
29.0
|
1.0
|
C
|
E:HIS161
|
4.8
|
29.2
|
1.0
|
NE2
|
E:HIS161
|
4.8
|
30.2
|
1.0
|
CA
|
E:LEU142
|
4.9
|
29.8
|
1.0
|
SG
|
E:CYS139
|
4.9
|
28.1
|
1.0
|
|
Reference:
L.Esser,
B.Quinn,
Y.F.Li,
M.Zhang,
M.Elberry,
L.Yu,
C.A.Yu,
D.Xia.
Crystallographic Studies of Quinol Oxidation Site Inhibitors: A Modified Classification of Inhibitors For the Cytochrome Bc(1) Complex. J.Mol.Biol. V. 341 281 2004.
ISSN: ISSN 0022-2836
PubMed: 15312779
DOI: 10.1016/J.JMB.2004.05.065
Page generated: Sat Aug 3 14:50:29 2024
|