Iron in PDB 9jqa: Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions
Enzymatic activity of Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions
All present enzymatic activity of Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions:
1.1.99.11;
Iron Binding Sites:
The binding sites of Iron atom in the Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions
(pdb code 9jqa). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 5 binding sites of Iron where determined in the
Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions, PDB code: 9jqa:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
Iron binding site 1 out
of 5 in 9jqa
Go back to
Iron Binding Sites List in 9jqa
Iron binding site 1 out
of 5 in the Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe602
b:89.9
occ:1.00
|
FE1
|
A:F3S602
|
0.0
|
89.9
|
1.0
|
S3
|
A:F3S602
|
2.3
|
65.7
|
1.0
|
S2
|
A:F3S602
|
2.3
|
67.8
|
1.0
|
S1
|
A:F3S602
|
2.3
|
62.6
|
1.0
|
SG
|
A:CYS226
|
2.3
|
62.7
|
1.0
|
FE4
|
A:F3S602
|
2.6
|
91.2
|
1.0
|
FE3
|
A:F3S602
|
2.6
|
91.2
|
1.0
|
CB
|
A:CYS226
|
3.2
|
56.9
|
1.0
|
S4
|
A:F3S602
|
3.8
|
69.5
|
1.0
|
CA
|
A:CYS226
|
3.9
|
53.0
|
1.0
|
CB
|
A:ASN219
|
4.1
|
52.5
|
1.0
|
CB
|
A:ALA230
|
4.2
|
53.5
|
1.0
|
OD1
|
A:ASN219
|
4.4
|
60.1
|
1.0
|
CD
|
A:PRO227
|
4.5
|
56.8
|
1.0
|
CG1
|
A:ILE228
|
4.6
|
57.9
|
1.0
|
N
|
A:ALA230
|
4.6
|
61.1
|
1.0
|
CG
|
A:MET231
|
4.6
|
60.1
|
1.0
|
N
|
A:ASN219
|
4.7
|
52.8
|
1.0
|
C
|
A:CYS226
|
4.7
|
62.5
|
1.0
|
CG
|
A:ASN219
|
4.8
|
61.0
|
1.0
|
SD
|
A:MET231
|
4.8
|
67.6
|
1.0
|
SG
|
A:CYS216
|
4.8
|
58.1
|
1.0
|
SG
|
A:CYS222
|
4.8
|
64.2
|
1.0
|
N
|
A:PRO227
|
4.9
|
64.1
|
1.0
|
N
|
A:MET231
|
4.9
|
70.4
|
1.0
|
CA
|
A:ALA230
|
4.9
|
55.1
|
1.0
|
CA
|
A:ASN219
|
4.9
|
48.9
|
1.0
|
|
Iron binding site 2 out
of 5 in 9jqa
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Iron Binding Sites List in 9jqa
Iron binding site 2 out
of 5 in the Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe602
b:91.2
occ:1.00
|
FE3
|
A:F3S602
|
0.0
|
91.2
|
1.0
|
S4
|
A:F3S602
|
2.3
|
69.5
|
1.0
|
S1
|
A:F3S602
|
2.3
|
62.6
|
1.0
|
S3
|
A:F3S602
|
2.3
|
65.7
|
1.0
|
SG
|
A:CYS222
|
2.3
|
64.2
|
1.0
|
FE4
|
A:F3S602
|
2.6
|
91.2
|
1.0
|
FE1
|
A:F3S602
|
2.6
|
89.9
|
1.0
|
CB
|
A:CYS222
|
3.5
|
58.0
|
1.0
|
N
|
A:CYS222
|
3.5
|
60.8
|
1.0
|
CA
|
A:CYS222
|
3.7
|
56.9
|
1.0
|
NE
|
A:ARG205
|
3.8
|
61.9
|
1.0
|
S2
|
A:F3S602
|
3.9
|
67.8
|
1.0
|
N
|
A:ASN220
|
4.1
|
61.3
|
1.0
|
N
|
A:ASN221
|
4.1
|
59.9
|
1.0
|
SD
|
A:MET231
|
4.3
|
67.6
|
1.0
|
CD
|
A:ARG205
|
4.4
|
51.8
|
1.0
|
C
|
A:ASN221
|
4.4
|
55.2
|
1.0
|
CZ
|
A:ARG205
|
4.5
|
56.9
|
1.0
|
NH2
|
A:ARG205
|
4.6
|
55.4
|
1.0
|
SG
|
A:CYS216
|
4.6
|
58.1
|
1.0
|
SG
|
A:CYS226
|
4.6
|
62.7
|
1.0
|
CB
|
A:SER343
|
4.7
|
62.0
|
1.0
|
CA
|
A:ASN220
|
4.7
|
57.3
|
1.0
|
CB
|
A:CYS226
|
4.7
|
56.9
|
1.0
|
CA
|
A:SER343
|
4.7
|
59.5
|
1.0
|
N
|
A:ASN219
|
4.8
|
52.8
|
1.0
|
C
|
A:ASN219
|
4.9
|
58.6
|
1.0
|
C
|
A:ASN220
|
4.9
|
66.9
|
1.0
|
CA
|
A:ASN221
|
4.9
|
54.2
|
1.0
|
CB
|
A:ASN219
|
4.9
|
52.5
|
1.0
|
CG
|
A:MET231
|
5.0
|
60.1
|
1.0
|
|
Iron binding site 3 out
of 5 in 9jqa
Go back to
Iron Binding Sites List in 9jqa
Iron binding site 3 out
of 5 in the Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe602
b:91.2
occ:1.00
|
FE4
|
A:F3S602
|
0.0
|
91.2
|
1.0
|
S3
|
A:F3S602
|
2.3
|
65.7
|
1.0
|
S2
|
A:F3S602
|
2.3
|
67.8
|
1.0
|
S4
|
A:F3S602
|
2.3
|
69.5
|
1.0
|
SG
|
A:CYS216
|
2.3
|
58.1
|
1.0
|
FE1
|
A:F3S602
|
2.6
|
89.9
|
1.0
|
FE3
|
A:F3S602
|
2.6
|
91.2
|
1.0
|
CB
|
A:CYS216
|
3.6
|
58.2
|
1.0
|
S1
|
A:F3S602
|
3.8
|
62.6
|
1.0
|
N
|
A:GLY218
|
3.9
|
56.7
|
1.0
|
N
|
A:ASN219
|
3.9
|
52.8
|
1.0
|
CD
|
A:ARG205
|
4.0
|
51.8
|
1.0
|
CA
|
A:CYS216
|
4.0
|
56.5
|
1.0
|
CA
|
A:GLY218
|
4.2
|
51.3
|
1.0
|
NE
|
A:ARG205
|
4.2
|
61.9
|
1.0
|
N
|
A:CYS217
|
4.3
|
60.0
|
1.0
|
CB
|
A:ALA230
|
4.3
|
53.5
|
1.0
|
CG
|
A:ARG205
|
4.5
|
59.9
|
1.0
|
C
|
A:CYS216
|
4.5
|
59.4
|
1.0
|
C
|
A:GLY218
|
4.5
|
55.6
|
1.0
|
SG
|
A:CYS222
|
4.6
|
64.2
|
1.0
|
SG
|
A:CYS226
|
4.7
|
62.7
|
1.0
|
CB
|
A:ASN219
|
4.8
|
52.5
|
1.0
|
N
|
A:ASN220
|
4.8
|
61.3
|
1.0
|
CA
|
A:ASN219
|
4.9
|
48.9
|
1.0
|
C
|
A:CYS217
|
4.9
|
63.9
|
1.0
|
|
Iron binding site 4 out
of 5 in 9jqa
Go back to
Iron Binding Sites List in 9jqa
Iron binding site 4 out
of 5 in the Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe501
b:89.7
occ:1.00
|
FE
|
C:HEC501
|
0.0
|
89.7
|
1.0
|
NB
|
C:HEC501
|
2.0
|
74.4
|
1.0
|
NC
|
C:HEC501
|
2.0
|
71.1
|
1.0
|
NA
|
C:HEC501
|
2.0
|
69.3
|
1.0
|
ND
|
C:HEC501
|
2.0
|
71.5
|
1.0
|
NE2
|
C:HIS347
|
2.0
|
64.9
|
1.0
|
SD
|
C:MET395
|
2.8
|
70.1
|
1.0
|
CD2
|
C:HIS347
|
2.9
|
59.3
|
1.0
|
C4B
|
C:HEC501
|
3.0
|
68.6
|
1.0
|
C1B
|
C:HEC501
|
3.0
|
63.4
|
1.0
|
C1C
|
C:HEC501
|
3.0
|
66.8
|
1.0
|
C1D
|
C:HEC501
|
3.0
|
64.9
|
1.0
|
C4D
|
C:HEC501
|
3.0
|
64.1
|
1.0
|
C4A
|
C:HEC501
|
3.0
|
64.7
|
1.0
|
C4C
|
C:HEC501
|
3.0
|
62.3
|
1.0
|
C1A
|
C:HEC501
|
3.0
|
65.7
|
1.0
|
CE1
|
C:HIS347
|
3.1
|
61.8
|
1.0
|
CG
|
C:MET395
|
3.2
|
56.6
|
1.0
|
CHD
|
C:HEC501
|
3.4
|
64.4
|
1.0
|
CHB
|
C:HEC501
|
3.4
|
63.5
|
1.0
|
CHA
|
C:HEC501
|
3.4
|
63.3
|
1.0
|
CHC
|
C:HEC501
|
3.4
|
61.8
|
1.0
|
CE
|
C:MET395
|
3.7
|
60.1
|
1.0
|
CG
|
C:HIS347
|
4.1
|
66.9
|
1.0
|
ND1
|
C:HIS347
|
4.2
|
69.1
|
1.0
|
C3B
|
C:HEC501
|
4.2
|
75.6
|
1.0
|
C2B
|
C:HEC501
|
4.2
|
65.5
|
1.0
|
C3C
|
C:HEC501
|
4.2
|
71.1
|
1.0
|
C2D
|
C:HEC501
|
4.2
|
67.4
|
1.0
|
C3D
|
C:HEC501
|
4.3
|
68.5
|
1.0
|
C3A
|
C:HEC501
|
4.3
|
68.4
|
1.0
|
C2C
|
C:HEC501
|
4.3
|
67.9
|
1.0
|
C2A
|
C:HEC501
|
4.3
|
68.2
|
1.0
|
CB
|
C:MET395
|
4.3
|
62.9
|
1.0
|
|
Iron binding site 5 out
of 5 in 9jqa
Go back to
Iron Binding Sites List in 9jqa
Iron binding site 5 out
of 5 in the Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Cryo-Em Structure of Fructose Dehydrogenase Variant From Gluconobacter Japonicus Truncating Heme 1C and C-Terminal Hydrophobic Regions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe502
b:95.5
occ:1.00
|
FE
|
C:HEC502
|
0.0
|
95.5
|
1.0
|
NB
|
C:HEC502
|
2.0
|
79.2
|
1.0
|
NC
|
C:HEC502
|
2.0
|
76.3
|
1.0
|
NA
|
C:HEC502
|
2.0
|
76.8
|
1.0
|
ND
|
C:HEC502
|
2.0
|
80.7
|
1.0
|
NE2
|
C:HIS205
|
2.0
|
74.2
|
1.0
|
SD
|
C:MET267
|
2.8
|
70.9
|
1.0
|
CD2
|
C:HIS205
|
2.9
|
71.0
|
1.0
|
C1B
|
C:HEC502
|
3.0
|
75.1
|
1.0
|
C4B
|
C:HEC502
|
3.0
|
72.7
|
1.0
|
C1D
|
C:HEC502
|
3.0
|
76.6
|
1.0
|
C1C
|
C:HEC502
|
3.0
|
76.0
|
1.0
|
C4A
|
C:HEC502
|
3.0
|
72.9
|
1.0
|
C4D
|
C:HEC502
|
3.0
|
74.5
|
1.0
|
C4C
|
C:HEC502
|
3.0
|
74.9
|
1.0
|
C1A
|
C:HEC502
|
3.0
|
73.2
|
1.0
|
CE
|
C:MET267
|
3.1
|
64.2
|
1.0
|
CE1
|
C:HIS205
|
3.1
|
69.4
|
1.0
|
CHD
|
C:HEC502
|
3.4
|
74.3
|
1.0
|
CHB
|
C:HEC502
|
3.4
|
76.2
|
1.0
|
CHA
|
C:HEC502
|
3.4
|
72.5
|
1.0
|
CHC
|
C:HEC502
|
3.4
|
75.6
|
1.0
|
CG
|
C:MET267
|
3.6
|
69.6
|
1.0
|
CG
|
C:HIS205
|
4.1
|
68.8
|
1.0
|
ND1
|
C:HIS205
|
4.1
|
68.5
|
1.0
|
C3B
|
C:HEC502
|
4.2
|
75.9
|
1.0
|
C2B
|
C:HEC502
|
4.2
|
76.4
|
1.0
|
C2D
|
C:HEC502
|
4.2
|
75.9
|
1.0
|
C3C
|
C:HEC502
|
4.2
|
80.6
|
1.0
|
C3A
|
C:HEC502
|
4.3
|
73.1
|
1.0
|
C3D
|
C:HEC502
|
4.3
|
74.3
|
1.0
|
C2A
|
C:HEC502
|
4.3
|
74.8
|
1.0
|
C2C
|
C:HEC502
|
4.3
|
75.7
|
1.0
|
CB
|
C:MET267
|
4.4
|
67.3
|
1.0
|
CA
|
C:MET267
|
4.9
|
65.1
|
1.0
|
|
Reference:
T.Adachi,
K.Ichikawa,
T.Miyata,
F.Makino,
H.Tanaka,
K.Namba,
K.Sowa.
Improved Direct Bioelectrochemical Fructose Oxidation with Surfactant-Free Heterotrimeric Fructose Dehydrogenase Variant Truncating Heme 1C and C-Terminal Hydrophobic Regions Acs Electrochem 2025.
DOI: 10.1021/ACSELECTROCHEM.5C00106
Page generated: Sat Aug 23 03:27:58 2025
|