Iron in PDB 1qob: Ferredoxin Mutation D62K
Protein crystallography data
The structure of Ferredoxin Mutation D62K, PDB code: 1qob
was solved by
H.M.Holden,
M.M.Benning,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
25.00 /
1.80
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
37.730,
38.230,
148.160,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.8 /
n/a
|
Iron Binding Sites:
The binding sites of Iron atom in the Ferredoxin Mutation D62K
(pdb code 1qob). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Ferredoxin Mutation D62K, PDB code: 1qob:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 1qob
Go back to
Iron Binding Sites List in 1qob
Iron binding site 1 out
of 4 in the Ferredoxin Mutation D62K
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Ferredoxin Mutation D62K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe100
b:19.3
occ:1.00
|
FE1
|
A:FES100
|
0.0
|
19.3
|
1.0
|
S1
|
A:FES100
|
2.2
|
19.5
|
1.0
|
S2
|
A:FES100
|
2.2
|
21.3
|
1.0
|
SG
|
A:CYS46
|
2.3
|
20.7
|
1.0
|
SG
|
A:CYS41
|
2.3
|
21.0
|
1.0
|
FE2
|
A:FES100
|
2.7
|
19.2
|
1.0
|
CB
|
A:CYS46
|
3.3
|
22.4
|
1.0
|
N
|
A:CYS46
|
3.5
|
17.8
|
1.0
|
CB
|
A:CYS41
|
3.5
|
18.9
|
1.0
|
N
|
A:CYS41
|
3.6
|
14.9
|
1.0
|
N
|
A:ARG42
|
3.7
|
19.8
|
1.0
|
CA
|
A:CYS46
|
3.7
|
16.1
|
1.0
|
CA
|
A:CYS41
|
3.9
|
17.1
|
1.0
|
C
|
A:CYS46
|
4.0
|
26.5
|
1.0
|
O
|
A:CYS46
|
4.1
|
20.6
|
1.0
|
N
|
A:ALA45
|
4.2
|
24.5
|
1.0
|
C
|
A:CYS41
|
4.2
|
37.9
|
1.0
|
SG
|
A:CYS79
|
4.3
|
19.5
|
1.0
|
N
|
A:ALA43
|
4.3
|
14.2
|
1.0
|
N
|
A:GLY44
|
4.3
|
17.6
|
1.0
|
C
|
A:ALA45
|
4.4
|
30.9
|
1.0
|
SG
|
A:CYS49
|
4.5
|
18.3
|
1.0
|
CA
|
A:ARG42
|
4.6
|
17.2
|
1.0
|
N
|
A:SER40
|
4.6
|
21.1
|
1.0
|
N
|
A:SER47
|
4.6
|
16.4
|
1.0
|
C
|
A:SER40
|
4.7
|
11.0
|
1.0
|
N
|
A:THR48
|
4.7
|
15.8
|
1.0
|
CA
|
A:GLY44
|
4.8
|
14.3
|
1.0
|
CA
|
A:ALA45
|
4.9
|
23.2
|
1.0
|
CB
|
A:SER40
|
4.9
|
24.8
|
1.0
|
C
|
A:GLY44
|
4.9
|
22.1
|
1.0
|
N
|
A:CYS49
|
5.0
|
17.4
|
1.0
|
|
Iron binding site 2 out
of 4 in 1qob
Go back to
Iron Binding Sites List in 1qob
Iron binding site 2 out
of 4 in the Ferredoxin Mutation D62K
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Ferredoxin Mutation D62K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe100
b:19.2
occ:1.00
|
FE2
|
A:FES100
|
0.0
|
19.2
|
1.0
|
S1
|
A:FES100
|
2.2
|
19.5
|
1.0
|
S2
|
A:FES100
|
2.2
|
21.3
|
1.0
|
SG
|
A:CYS79
|
2.3
|
19.5
|
1.0
|
SG
|
A:CYS49
|
2.3
|
18.3
|
1.0
|
FE1
|
A:FES100
|
2.7
|
19.3
|
1.0
|
CB
|
A:CYS79
|
3.2
|
17.6
|
1.0
|
CB
|
A:CYS49
|
3.2
|
13.2
|
1.0
|
N
|
A:CYS79
|
4.2
|
18.6
|
1.0
|
N
|
A:CYS49
|
4.2
|
17.4
|
1.0
|
N
|
A:GLY44
|
4.3
|
17.6
|
1.0
|
CA
|
A:CYS79
|
4.3
|
13.7
|
1.0
|
N
|
A:ARG42
|
4.3
|
19.8
|
1.0
|
CA
|
A:CYS49
|
4.4
|
20.5
|
1.0
|
SG
|
A:CYS41
|
4.4
|
21.0
|
1.0
|
CA
|
A:ARG42
|
4.5
|
17.2
|
1.0
|
SG
|
A:CYS46
|
4.5
|
20.7
|
1.0
|
CB
|
A:LEU77
|
4.6
|
22.8
|
1.0
|
N
|
A:ALA43
|
4.6
|
14.2
|
1.0
|
CA
|
A:GLY44
|
4.6
|
14.3
|
1.0
|
C
|
A:ARG42
|
4.9
|
16.7
|
1.0
|
O
|
A:CYS46
|
4.9
|
20.6
|
1.0
|
|
Iron binding site 3 out
of 4 in 1qob
Go back to
Iron Binding Sites List in 1qob
Iron binding site 3 out
of 4 in the Ferredoxin Mutation D62K
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Ferredoxin Mutation D62K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe100
b:21.5
occ:1.00
|
FE1
|
B:FES100
|
0.0
|
21.5
|
1.0
|
SG
|
B:CYS46
|
2.1
|
20.5
|
1.0
|
S2
|
B:FES100
|
2.2
|
19.2
|
1.0
|
S1
|
B:FES100
|
2.2
|
18.1
|
1.0
|
SG
|
B:CYS41
|
2.2
|
20.2
|
1.0
|
FE2
|
B:FES100
|
2.7
|
20.0
|
1.0
|
CB
|
B:CYS46
|
3.3
|
18.4
|
1.0
|
CB
|
B:CYS41
|
3.4
|
26.0
|
1.0
|
N
|
B:CYS46
|
3.5
|
25.7
|
1.0
|
N
|
B:CYS41
|
3.6
|
22.2
|
1.0
|
CA
|
B:CYS46
|
3.7
|
21.3
|
1.0
|
N
|
B:ARG42
|
3.7
|
15.9
|
1.0
|
CA
|
B:CYS41
|
3.9
|
22.0
|
1.0
|
C
|
B:CYS46
|
4.0
|
18.9
|
1.0
|
O
|
B:CYS46
|
4.1
|
20.7
|
1.0
|
C
|
B:CYS41
|
4.2
|
21.8
|
1.0
|
N
|
B:ALA45
|
4.2
|
16.4
|
1.0
|
SG
|
B:CYS79
|
4.3
|
19.2
|
1.0
|
N
|
B:GLY44
|
4.4
|
17.6
|
1.0
|
C
|
B:ALA45
|
4.4
|
23.4
|
1.0
|
N
|
B:ALA43
|
4.4
|
21.3
|
1.0
|
SG
|
B:CYS49
|
4.5
|
21.7
|
1.0
|
N
|
B:SER40
|
4.6
|
20.7
|
1.0
|
CA
|
B:ARG42
|
4.7
|
17.1
|
1.0
|
C
|
B:SER40
|
4.7
|
29.1
|
1.0
|
N
|
B:SER47
|
4.7
|
16.0
|
1.0
|
N
|
B:THR48
|
4.8
|
20.8
|
1.0
|
CA
|
B:GLY44
|
4.8
|
21.2
|
1.0
|
C
|
B:GLY44
|
4.8
|
21.9
|
1.0
|
CA
|
B:ALA45
|
4.9
|
12.7
|
1.0
|
N
|
B:CYS49
|
4.9
|
18.0
|
1.0
|
CB
|
B:SER40
|
4.9
|
18.9
|
1.0
|
CA
|
B:SER40
|
5.0
|
15.9
|
1.0
|
|
Iron binding site 4 out
of 4 in 1qob
Go back to
Iron Binding Sites List in 1qob
Iron binding site 4 out
of 4 in the Ferredoxin Mutation D62K
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Ferredoxin Mutation D62K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe100
b:20.0
occ:1.00
|
FE2
|
B:FES100
|
0.0
|
20.0
|
1.0
|
S2
|
B:FES100
|
2.1
|
19.2
|
1.0
|
S1
|
B:FES100
|
2.2
|
18.1
|
1.0
|
SG
|
B:CYS49
|
2.2
|
21.7
|
1.0
|
SG
|
B:CYS79
|
2.2
|
19.2
|
1.0
|
FE1
|
B:FES100
|
2.7
|
21.5
|
1.0
|
CB
|
B:CYS79
|
3.2
|
14.7
|
1.0
|
CB
|
B:CYS49
|
3.4
|
17.9
|
1.0
|
N
|
B:CYS79
|
4.2
|
16.7
|
1.0
|
N
|
B:CYS49
|
4.2
|
18.0
|
1.0
|
CA
|
B:CYS79
|
4.2
|
20.0
|
1.0
|
N
|
B:GLY44
|
4.2
|
17.6
|
1.0
|
SG
|
B:CYS41
|
4.3
|
20.2
|
1.0
|
N
|
B:ARG42
|
4.3
|
15.9
|
1.0
|
CA
|
B:CYS49
|
4.4
|
14.4
|
1.0
|
CB
|
B:LEU77
|
4.5
|
14.9
|
1.0
|
SG
|
B:CYS46
|
4.5
|
20.5
|
1.0
|
CA
|
B:ARG42
|
4.5
|
17.1
|
1.0
|
CA
|
B:GLY44
|
4.5
|
21.2
|
1.0
|
N
|
B:ALA43
|
4.7
|
21.3
|
1.0
|
O
|
B:CYS46
|
4.9
|
20.7
|
1.0
|
C
|
B:ARG42
|
4.9
|
28.1
|
1.0
|
CA
|
B:LEU77
|
5.0
|
16.9
|
1.0
|
|
Reference:
J.K.Hurley,
A.M.Weber-Main,
M.T.Stankovich,
M.M.Benning,
J.B.Thoden,
J.L.Vanhooke,
H.M.Holden,
Y.K.Chae,
B.Xia,
H.Cheng,
J.L.Markley,
M.Martinez-Julvez,
C.Gomez-Moreno,
J.L.Schmeits,
G.Tollin.
Structure-Function Relationships in Anabaena Ferredoxin: Correlations Between X-Ray Crystal Structures, Reduction Potentials, and Rate Constants of Electron Transfer to Ferredoxin:Nadp+ Reductase For Site-Specific Ferredoxin Mutants. Biochemistry V. 36 11100 1997.
ISSN: ISSN 0006-2960
PubMed: 9287153
DOI: 10.1021/BI9709001
Page generated: Sat Aug 3 13:39:58 2024
|