Iron in PDB 4rwm: Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol
Enzymatic activity of Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol
All present enzymatic activity of Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol:
1.7.3.4;
Protein crystallography data
The structure of Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol, PDB code: 4rwm
was solved by
A.Dietl,
W.Maalcke,
T.R.M.Barends,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
20.00 /
1.80
|
|
Space group
|
P 21 3
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
130.290,
130.290,
130.290,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
14.7 /
16.4
|
Iron Binding Sites:
The binding sites of Iron atom in the Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol
(pdb code 4rwm). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the
Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol, PDB code: 4rwm:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 4rwm
Go back to
Iron Binding Sites List in 4rwm
Iron binding site 1 out
of 8 in the Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe610
b:16.8
occ:1.00
|
FE
|
A:HEM610
|
0.0
|
16.8
|
1.0
|
|
NE2
|
A:HIS120
|
2.0
|
16.8
|
1.0
|
|
NE2
|
A:HIS168
|
2.0
|
16.6
|
1.0
|
|
NB
|
A:HEM610
|
2.0
|
16.4
|
1.0
|
|
NC
|
A:HEM610
|
2.0
|
17.3
|
1.0
|
|
ND
|
A:HEM610
|
2.1
|
16.8
|
1.0
|
|
NA
|
A:HEM610
|
2.1
|
15.9
|
1.0
|
|
CE1
|
A:HIS120
|
3.0
|
16.8
|
1.0
|
|
CD2
|
A:HIS168
|
3.0
|
17.1
|
1.0
|
|
CE1
|
A:HIS168
|
3.0
|
17.1
|
1.0
|
|
CD2
|
A:HIS120
|
3.0
|
17.2
|
1.0
|
|
C1B
|
A:HEM610
|
3.0
|
17.1
|
1.0
|
|
C4C
|
A:HEM610
|
3.0
|
18.4
|
1.0
|
|
C1C
|
A:HEM610
|
3.0
|
18.2
|
1.0
|
|
C4B
|
A:HEM610
|
3.1
|
17.3
|
1.0
|
|
C1D
|
A:HEM610
|
3.1
|
17.4
|
1.0
|
|
C4A
|
A:HEM610
|
3.1
|
16.1
|
1.0
|
|
C1A
|
A:HEM610
|
3.1
|
16.2
|
1.0
|
|
C4D
|
A:HEM610
|
3.1
|
16.6
|
1.0
|
|
CHD
|
A:HEM610
|
3.4
|
17.7
|
1.0
|
|
CHB
|
A:HEM610
|
3.4
|
15.9
|
1.0
|
|
CHC
|
A:HEM610
|
3.4
|
17.5
|
1.0
|
|
CHA
|
A:HEM610
|
3.4
|
16.5
|
1.0
|
|
ND1
|
A:HIS120
|
4.1
|
16.3
|
1.0
|
|
ND1
|
A:HIS168
|
4.1
|
17.0
|
1.0
|
|
CG
|
A:HIS168
|
4.1
|
17.6
|
1.0
|
|
CG
|
A:HIS120
|
4.2
|
17.1
|
1.0
|
|
C3B
|
A:HEM610
|
4.3
|
17.3
|
1.0
|
|
C2B
|
A:HEM610
|
4.3
|
16.7
|
1.0
|
|
C2C
|
A:HEM610
|
4.3
|
18.6
|
1.0
|
|
C3C
|
A:HEM610
|
4.3
|
18.8
|
1.0
|
|
C2A
|
A:HEM610
|
4.3
|
16.0
|
1.0
|
|
C3A
|
A:HEM610
|
4.3
|
15.7
|
1.0
|
|
C2D
|
A:HEM610
|
4.3
|
17.6
|
1.0
|
|
C3D
|
A:HEM610
|
4.3
|
16.6
|
1.0
|
|
CD1
|
A:LEU171
|
5.0
|
16.9
|
1.0
|
|
Iron binding site 2 out
of 8 in 4rwm
Go back to
Iron Binding Sites List in 4rwm
Iron binding site 2 out
of 8 in the Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe611
b:15.0
occ:1.00
|
FE
|
A:HEM611
|
0.0
|
15.0
|
1.0
|
|
NE2
|
A:HIS164
|
2.0
|
15.8
|
1.0
|
|
NB
|
A:HEM611
|
2.0
|
14.6
|
1.0
|
|
NA
|
A:HEM611
|
2.0
|
14.4
|
1.0
|
|
NE2
|
A:HIS241
|
2.0
|
14.8
|
1.0
|
|
NC
|
A:HEM611
|
2.1
|
14.1
|
1.0
|
|
ND
|
A:HEM611
|
2.1
|
15.0
|
1.0
|
|
CE1
|
A:HIS164
|
3.0
|
16.0
|
1.0
|
|
CE1
|
A:HIS241
|
3.0
|
14.9
|
1.0
|
|
CD2
|
A:HIS241
|
3.0
|
14.6
|
1.0
|
|
C4A
|
A:HEM611
|
3.0
|
14.7
|
1.0
|
|
C4B
|
A:HEM611
|
3.0
|
14.4
|
1.0
|
|
C1B
|
A:HEM611
|
3.0
|
14.4
|
1.0
|
|
CD2
|
A:HIS164
|
3.1
|
16.2
|
1.0
|
|
C1A
|
A:HEM611
|
3.1
|
14.5
|
1.0
|
|
C1C
|
A:HEM611
|
3.1
|
13.9
|
1.0
|
|
C1D
|
A:HEM611
|
3.1
|
15.0
|
1.0
|
|
C4C
|
A:HEM611
|
3.1
|
14.6
|
1.0
|
|
C4D
|
A:HEM611
|
3.1
|
14.8
|
1.0
|
|
CHB
|
A:HEM611
|
3.4
|
14.1
|
1.0
|
|
CHC
|
A:HEM611
|
3.4
|
14.3
|
1.0
|
|
CHA
|
A:HEM611
|
3.4
|
14.4
|
1.0
|
|
CHD
|
A:HEM611
|
3.4
|
15.0
|
1.0
|
|
ND1
|
A:HIS164
|
4.1
|
15.9
|
1.0
|
|
ND1
|
A:HIS241
|
4.1
|
14.6
|
1.0
|
|
CG
|
A:HIS241
|
4.2
|
14.4
|
1.0
|
|
CG
|
A:HIS164
|
4.2
|
16.8
|
1.0
|
|
C3B
|
A:HEM611
|
4.3
|
14.9
|
1.0
|
|
C3A
|
A:HEM611
|
4.3
|
14.5
|
1.0
|
|
C2B
|
A:HEM611
|
4.3
|
14.6
|
1.0
|
|
C2A
|
A:HEM611
|
4.3
|
15.1
|
1.0
|
|
C2C
|
A:HEM611
|
4.3
|
14.3
|
1.0
|
|
C3C
|
A:HEM611
|
4.3
|
14.8
|
1.0
|
|
C2D
|
A:HEM611
|
4.3
|
15.3
|
1.0
|
|
C3D
|
A:HEM611
|
4.3
|
15.2
|
1.0
|
|
Iron binding site 3 out
of 8 in 4rwm
Go back to
Iron Binding Sites List in 4rwm
Iron binding site 3 out
of 8 in the Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe612
b:15.6
occ:1.00
|
FE
|
A:HEM612
|
0.0
|
15.6
|
1.0
|
|
NE2
|
A:HIS136
|
2.0
|
17.0
|
1.0
|
|
NE2
|
A:HIS183
|
2.0
|
13.7
|
1.0
|
|
NB
|
A:HEM612
|
2.0
|
14.9
|
1.0
|
|
NA
|
A:HEM612
|
2.0
|
14.9
|
1.0
|
|
NC
|
A:HEM612
|
2.0
|
15.4
|
1.0
|
|
ND
|
A:HEM612
|
2.1
|
15.4
|
1.0
|
|
CE1
|
A:HIS183
|
3.0
|
14.5
|
1.0
|
|
CE1
|
A:HIS136
|
3.0
|
17.1
|
1.0
|
|
CD2
|
A:HIS136
|
3.0
|
17.1
|
1.0
|
|
CD2
|
A:HIS183
|
3.0
|
14.0
|
1.0
|
|
C4C
|
A:HEM612
|
3.0
|
15.6
|
1.0
|
|
C1D
|
A:HEM612
|
3.0
|
15.3
|
1.0
|
|
C1B
|
A:HEM612
|
3.0
|
15.5
|
1.0
|
|
C4A
|
A:HEM612
|
3.1
|
14.5
|
1.0
|
|
C4D
|
A:HEM612
|
3.1
|
14.8
|
1.0
|
|
C1C
|
A:HEM612
|
3.1
|
15.1
|
1.0
|
|
C4B
|
A:HEM612
|
3.1
|
14.8
|
1.0
|
|
C1A
|
A:HEM612
|
3.1
|
14.5
|
1.0
|
|
CHD
|
A:HEM612
|
3.4
|
15.2
|
1.0
|
|
CHB
|
A:HEM612
|
3.4
|
14.7
|
1.0
|
|
CHA
|
A:HEM612
|
3.5
|
14.7
|
1.0
|
|
CHC
|
A:HEM612
|
3.5
|
15.1
|
1.0
|
|
ND1
|
A:HIS183
|
4.1
|
14.0
|
1.0
|
|
ND1
|
A:HIS136
|
4.1
|
17.2
|
1.0
|
|
CG
|
A:HIS183
|
4.2
|
14.1
|
1.0
|
|
CG
|
A:HIS136
|
4.2
|
18.4
|
1.0
|
|
C3C
|
A:HEM612
|
4.3
|
16.4
|
1.0
|
|
C2B
|
A:HEM612
|
4.3
|
15.7
|
1.0
|
|
C2C
|
A:HEM612
|
4.3
|
15.8
|
1.0
|
|
C2D
|
A:HEM612
|
4.3
|
15.5
|
1.0
|
|
C3A
|
A:HEM612
|
4.3
|
14.5
|
1.0
|
|
C3B
|
A:HEM612
|
4.3
|
15.8
|
1.0
|
|
C3D
|
A:HEM612
|
4.3
|
15.7
|
1.0
|
|
C2A
|
A:HEM612
|
4.3
|
15.1
|
1.0
|
|
O
|
A:HOH805
|
4.8
|
16.6
|
1.0
|
|
Iron binding site 4 out
of 8 in 4rwm
Go back to
Iron Binding Sites List in 4rwm
Iron binding site 4 out
of 8 in the Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe613
b:15.6
occ:1.00
|
FE
|
A:HEC613
|
0.0
|
15.6
|
1.0
|
|
NB
|
A:HEC613
|
1.9
|
15.3
|
1.0
|
|
NA
|
A:HEC613
|
1.9
|
16.3
|
1.0
|
|
ND
|
A:HEC613
|
1.9
|
15.5
|
1.0
|
|
NC
|
A:HEC613
|
1.9
|
15.4
|
1.0
|
|
NE2
|
A:HIS227
|
2.1
|
16.5
|
1.0
|
|
O
|
A:HOH1085
|
2.2
|
18.9
|
1.0
|
|
C1B
|
A:HEC613
|
2.9
|
15.1
|
1.0
|
|
C1C
|
A:HEC613
|
2.9
|
15.0
|
1.0
|
|
CE1
|
A:HIS227
|
2.9
|
16.4
|
1.0
|
|
C4A
|
A:HEC613
|
2.9
|
16.6
|
1.0
|
|
C4C
|
A:HEC613
|
3.0
|
15.1
|
1.0
|
|
C4D
|
A:HEC613
|
3.0
|
15.8
|
1.0
|
|
C1D
|
A:HEC613
|
3.0
|
14.9
|
1.0
|
|
C1A
|
A:HEC613
|
3.0
|
17.1
|
1.0
|
|
C4B
|
A:HEC613
|
3.0
|
15.5
|
1.0
|
|
CD2
|
A:HIS227
|
3.2
|
16.0
|
1.0
|
|
CHB
|
A:HEC613
|
3.3
|
15.8
|
1.0
|
|
CHD
|
A:HEC613
|
3.4
|
15.3
|
1.0
|
|
O1
|
A:EDO604
|
3.4
|
23.4
|
1.0
|
|
CHA
|
A:HEC613
|
3.4
|
16.7
|
1.0
|
|
CHC
|
A:HEC613
|
3.4
|
15.3
|
1.0
|
|
C1
|
A:EDO604
|
3.9
|
24.5
|
1.0
|
|
NE2
|
A:HIS263
|
4.0
|
15.7
|
1.0
|
|
ND1
|
A:HIS227
|
4.1
|
15.8
|
1.0
|
|
C2B
|
A:HEC613
|
4.1
|
14.5
|
1.0
|
|
C2D
|
A:HEC613
|
4.2
|
15.4
|
1.0
|
|
C3D
|
A:HEC613
|
4.2
|
15.3
|
1.0
|
|
C3A
|
A:HEC613
|
4.2
|
16.1
|
1.0
|
|
C2C
|
A:HEC613
|
4.2
|
15.0
|
1.0
|
|
C3B
|
A:HEC613
|
4.2
|
14.7
|
1.0
|
|
C3C
|
A:HEC613
|
4.2
|
14.6
|
1.0
|
|
CG
|
A:HIS227
|
4.2
|
15.2
|
1.0
|
|
C2A
|
A:HEC613
|
4.3
|
16.3
|
1.0
|
|
O2
|
A:EDO604
|
4.7
|
25.1
|
1.0
|
|
CD2
|
A:HIS263
|
4.8
|
16.4
|
1.0
|
|
C2
|
A:EDO604
|
4.9
|
25.1
|
1.0
|
|
Iron binding site 5 out
of 8 in 4rwm
Go back to
Iron Binding Sites List in 4rwm
Iron binding site 5 out
of 8 in the Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe614
b:13.6
occ:1.00
|
FE
|
A:HEM614
|
0.0
|
13.6
|
1.0
|
|
NB
|
A:HEM614
|
2.0
|
13.5
|
1.0
|
|
NE2
|
A:HIS311
|
2.0
|
13.2
|
1.0
|
|
NA
|
A:HEM614
|
2.0
|
13.8
|
1.0
|
|
NE2
|
A:HIS238
|
2.0
|
12.8
|
1.0
|
|
NC
|
A:HEM614
|
2.0
|
13.2
|
1.0
|
|
ND
|
A:HEM614
|
2.0
|
12.1
|
1.0
|
|
CD2
|
A:HIS311
|
3.0
|
12.5
|
1.0
|
|
CD2
|
A:HIS238
|
3.0
|
13.1
|
1.0
|
|
C1B
|
A:HEM614
|
3.0
|
13.0
|
1.0
|
|
C4A
|
A:HEM614
|
3.0
|
13.4
|
1.0
|
|
CE1
|
A:HIS238
|
3.0
|
13.1
|
1.0
|
|
C1D
|
A:HEM614
|
3.0
|
13.1
|
1.0
|
|
CE1
|
A:HIS311
|
3.1
|
13.4
|
1.0
|
|
C4B
|
A:HEM614
|
3.1
|
13.1
|
1.0
|
|
C4C
|
A:HEM614
|
3.1
|
12.4
|
1.0
|
|
C1A
|
A:HEM614
|
3.1
|
13.4
|
1.0
|
|
C4D
|
A:HEM614
|
3.1
|
12.7
|
1.0
|
|
C1C
|
A:HEM614
|
3.1
|
13.3
|
1.0
|
|
CHB
|
A:HEM614
|
3.4
|
12.7
|
1.0
|
|
CHD
|
A:HEM614
|
3.4
|
12.0
|
1.0
|
|
CHA
|
A:HEM614
|
3.5
|
13.0
|
1.0
|
|
CHC
|
A:HEM614
|
3.5
|
13.0
|
1.0
|
|
CG
|
A:HIS311
|
4.1
|
13.6
|
1.0
|
|
ND1
|
A:HIS311
|
4.1
|
12.8
|
1.0
|
|
ND1
|
A:HIS238
|
4.1
|
13.3
|
1.0
|
|
CG
|
A:HIS238
|
4.2
|
12.7
|
1.0
|
|
C2B
|
A:HEM614
|
4.2
|
12.5
|
1.0
|
|
C3B
|
A:HEM614
|
4.2
|
12.9
|
1.0
|
|
C3A
|
A:HEM614
|
4.3
|
13.2
|
1.0
|
|
C3C
|
A:HEM614
|
4.3
|
11.9
|
1.0
|
|
C2A
|
A:HEM614
|
4.3
|
13.8
|
1.0
|
|
C2D
|
A:HEM614
|
4.3
|
12.5
|
1.0
|
|
C2C
|
A:HEM614
|
4.3
|
12.9
|
1.0
|
|
C3D
|
A:HEM614
|
4.3
|
13.2
|
1.0
|
|
O
|
A:HOH1168
|
4.7
|
12.1
|
1.0
|
|
CG
|
A:GLU186
|
4.9
|
15.2
|
1.0
|
|
CE
|
A:MET306
|
5.0
|
15.0
|
1.0
|
|
Iron binding site 6 out
of 8 in 4rwm
Go back to
Iron Binding Sites List in 4rwm
Iron binding site 6 out
of 8 in the Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe615
b:13.6
occ:1.00
|
FE
|
A:HEM615
|
0.0
|
13.6
|
1.0
|
|
NE2
|
A:HIS258
|
2.0
|
15.0
|
1.0
|
|
NB
|
A:HEM615
|
2.0
|
12.1
|
1.0
|
|
NE2
|
A:HIS198
|
2.0
|
12.1
|
1.0
|
|
ND
|
A:HEM615
|
2.0
|
13.2
|
1.0
|
|
NC
|
A:HEM615
|
2.0
|
12.3
|
1.0
|
|
NA
|
A:HEM615
|
2.1
|
12.9
|
1.0
|
|
CE1
|
A:HIS258
|
3.0
|
15.0
|
1.0
|
|
CD2
|
A:HIS198
|
3.0
|
12.8
|
1.0
|
|
CE1
|
A:HIS198
|
3.0
|
13.3
|
1.0
|
|
C1B
|
A:HEM615
|
3.0
|
12.5
|
1.0
|
|
C4B
|
A:HEM615
|
3.0
|
12.6
|
1.0
|
|
C1D
|
A:HEM615
|
3.0
|
12.8
|
1.0
|
|
C4D
|
A:HEM615
|
3.1
|
14.1
|
1.0
|
|
C1C
|
A:HEM615
|
3.1
|
12.3
|
1.0
|
|
CD2
|
A:HIS258
|
3.1
|
14.8
|
1.0
|
|
C1A
|
A:HEM615
|
3.1
|
13.4
|
1.0
|
|
C4C
|
A:HEM615
|
3.1
|
12.8
|
1.0
|
|
C4A
|
A:HEM615
|
3.1
|
13.4
|
1.0
|
|
CHC
|
A:HEM615
|
3.4
|
11.9
|
1.0
|
|
CHD
|
A:HEM615
|
3.4
|
12.5
|
1.0
|
|
CHA
|
A:HEM615
|
3.4
|
13.5
|
1.0
|
|
CHB
|
A:HEM615
|
3.4
|
12.8
|
1.0
|
|
ND1
|
A:HIS258
|
4.1
|
14.7
|
1.0
|
|
ND1
|
A:HIS198
|
4.1
|
12.5
|
1.0
|
|
CG
|
A:HIS198
|
4.1
|
12.7
|
1.0
|
|
CG
|
A:HIS258
|
4.2
|
14.4
|
1.0
|
|
C2B
|
A:HEM615
|
4.2
|
12.3
|
1.0
|
|
C3B
|
A:HEM615
|
4.3
|
12.5
|
1.0
|
|
C3D
|
A:HEM615
|
4.3
|
15.2
|
1.0
|
|
C2D
|
A:HEM615
|
4.3
|
13.9
|
1.0
|
|
C2A
|
A:HEM615
|
4.3
|
14.0
|
1.0
|
|
C2C
|
A:HEM615
|
4.3
|
12.4
|
1.0
|
|
C3A
|
A:HEM615
|
4.3
|
13.5
|
1.0
|
|
C3C
|
A:HEM615
|
4.3
|
12.1
|
1.0
|
|
O
|
A:HOH1162
|
4.9
|
14.7
|
1.0
|
|
Iron binding site 7 out
of 8 in 4rwm
Go back to
Iron Binding Sites List in 4rwm
Iron binding site 7 out
of 8 in the Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe616
b:13.2
occ:1.00
|
FE
|
A:HEM616
|
0.0
|
13.2
|
1.0
|
|
NB
|
A:HEM616
|
2.0
|
12.8
|
1.0
|
|
NA
|
A:HEM616
|
2.0
|
13.4
|
1.0
|
|
NE2
|
A:HIS305
|
2.0
|
13.5
|
1.0
|
|
NE2
|
A:HIS443
|
2.0
|
13.2
|
1.0
|
|
NC
|
A:HEM616
|
2.1
|
12.3
|
1.0
|
|
ND
|
A:HEM616
|
2.1
|
13.0
|
1.0
|
|
CD2
|
A:HIS443
|
3.0
|
13.9
|
1.0
|
|
CE1
|
A:HIS305
|
3.0
|
14.1
|
1.0
|
|
C1B
|
A:HEM616
|
3.0
|
12.4
|
1.0
|
|
C4B
|
A:HEM616
|
3.0
|
12.2
|
1.0
|
|
C4A
|
A:HEM616
|
3.0
|
12.7
|
1.0
|
|
C1A
|
A:HEM616
|
3.0
|
13.5
|
1.0
|
|
CD2
|
A:HIS305
|
3.0
|
13.8
|
1.0
|
|
CE1
|
A:HIS443
|
3.1
|
14.6
|
1.0
|
|
C1D
|
A:HEM616
|
3.1
|
12.2
|
1.0
|
|
C1C
|
A:HEM616
|
3.1
|
11.8
|
1.0
|
|
C4C
|
A:HEM616
|
3.1
|
11.8
|
1.0
|
|
C4D
|
A:HEM616
|
3.1
|
13.3
|
1.0
|
|
CHB
|
A:HEM616
|
3.4
|
12.9
|
1.0
|
|
CHC
|
A:HEM616
|
3.4
|
11.8
|
1.0
|
|
CHA
|
A:HEM616
|
3.4
|
13.5
|
1.0
|
|
CHD
|
A:HEM616
|
3.4
|
11.7
|
1.0
|
|
ND1
|
A:HIS305
|
4.1
|
12.8
|
1.0
|
|
CG
|
A:HIS443
|
4.1
|
13.0
|
1.0
|
|
ND1
|
A:HIS443
|
4.1
|
13.7
|
1.0
|
|
CG
|
A:HIS305
|
4.2
|
13.5
|
1.0
|
|
C3B
|
A:HEM616
|
4.2
|
12.1
|
1.0
|
|
C2B
|
A:HEM616
|
4.2
|
12.3
|
1.0
|
|
C3A
|
A:HEM616
|
4.2
|
14.5
|
1.0
|
|
C2A
|
A:HEM616
|
4.2
|
13.5
|
1.0
|
|
C2C
|
A:HEM616
|
4.3
|
12.4
|
1.0
|
|
C3C
|
A:HEM616
|
4.3
|
11.7
|
1.0
|
|
C2D
|
A:HEM616
|
4.3
|
12.3
|
1.0
|
|
C3D
|
A:HEM616
|
4.3
|
13.0
|
1.0
|
|
Iron binding site 8 out
of 8 in 4rwm
Go back to
Iron Binding Sites List in 4rwm
Iron binding site 8 out
of 8 in the Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Kuenenia Stuttgartiensis Hydroxylamine Oxidoreductase Cryoprotected with Ethylene Glycol within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe617
b:13.4
occ:1.00
|
FE
|
A:HEM617
|
0.0
|
13.4
|
1.0
|
|
NE2
|
A:HIS350
|
2.0
|
14.0
|
1.0
|
|
NC
|
A:HEM617
|
2.0
|
13.9
|
1.0
|
|
NE2
|
A:HIS274
|
2.0
|
13.1
|
1.0
|
|
NB
|
A:HEM617
|
2.0
|
13.3
|
1.0
|
|
ND
|
A:HEM617
|
2.0
|
12.9
|
1.0
|
|
NA
|
A:HEM617
|
2.0
|
13.8
|
1.0
|
|
CE1
|
A:HIS274
|
2.9
|
13.1
|
1.0
|
|
CD2
|
A:HIS350
|
3.0
|
14.0
|
1.0
|
|
CE1
|
A:HIS350
|
3.0
|
14.2
|
1.0
|
|
C1C
|
A:HEM617
|
3.0
|
13.4
|
1.0
|
|
C4C
|
A:HEM617
|
3.0
|
13.1
|
1.0
|
|
C1D
|
A:HEM617
|
3.0
|
11.9
|
1.0
|
|
C1A
|
A:HEM617
|
3.1
|
13.6
|
1.0
|
|
C4B
|
A:HEM617
|
3.1
|
13.9
|
1.0
|
|
C4A
|
A:HEM617
|
3.1
|
13.1
|
1.0
|
|
C1B
|
A:HEM617
|
3.1
|
13.5
|
1.0
|
|
C4D
|
A:HEM617
|
3.1
|
13.0
|
1.0
|
|
CD2
|
A:HIS274
|
3.1
|
12.9
|
1.0
|
|
CHD
|
A:HEM617
|
3.4
|
12.6
|
1.0
|
|
CHC
|
A:HEM617
|
3.4
|
13.2
|
1.0
|
|
CHA
|
A:HEM617
|
3.4
|
13.0
|
1.0
|
|
CHB
|
A:HEM617
|
3.4
|
13.6
|
1.0
|
|
ND1
|
A:HIS274
|
4.1
|
12.5
|
1.0
|
|
ND1
|
A:HIS350
|
4.1
|
14.1
|
1.0
|
|
CG
|
A:HIS350
|
4.1
|
14.0
|
1.0
|
|
CG
|
A:HIS274
|
4.2
|
12.3
|
1.0
|
|
C2C
|
A:HEM617
|
4.3
|
13.4
|
1.0
|
|
C3C
|
A:HEM617
|
4.3
|
13.3
|
1.0
|
|
C2A
|
A:HEM617
|
4.3
|
13.2
|
1.0
|
|
C3A
|
A:HEM617
|
4.3
|
12.9
|
1.0
|
|
C3B
|
A:HEM617
|
4.3
|
14.1
|
1.0
|
|
C2D
|
A:HEM617
|
4.3
|
12.2
|
1.0
|
|
C2B
|
A:HEM617
|
4.3
|
14.5
|
1.0
|
|
C3D
|
A:HEM617
|
4.3
|
12.7
|
1.0
|
|
O
|
A:HOH909
|
4.8
|
14.5
|
1.0
|
|
Reference:
A.Dietl,
W.Maalcke,
T.R.Barends.
An Unexpected Reactivity of the P460 Cofactor in Hydroxylamine Oxidoreductase. Acta Crystallogr. D Biol. V. 71 1708 2015CRYSTALLOGR..
ISSN: ESSN 1399-0047
PubMed: 26249351
DOI: 10.1107/S1399004715010706
Page generated: Sun Dec 13 15:46:22 2020
|
