Iron in PDB 3use: Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
Enzymatic activity of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
All present enzymatic activity of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form:
1.12.99.6;
Protein crystallography data
The structure of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form, PDB code: 3use
was solved by
A.Volbeda,
J.C.Fontecilla-Camps,
C.Darnault,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.82 /
1.67
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
93.930,
97.790,
183.290,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
12 /
16.8
|
Other elements in 3use:
The structure of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form also contains other interesting chemical elements:
Iron Binding Sites:
Iron binding site 1 out
of 32 in 3use
Go back to
Iron Binding Sites List in 3use
Iron binding site 1 out
of 32 in the Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe401
b:8.0
occ:1.00
|
FE1
|
S:SF4401
|
0.0
|
8.0
|
1.0
|
S3
|
S:SF4401
|
2.3
|
8.3
|
1.0
|
S4
|
S:SF4401
|
2.3
|
8.3
|
1.0
|
SG
|
S:CYS215
|
2.3
|
8.8
|
1.0
|
S2
|
S:SF4401
|
2.3
|
7.7
|
1.0
|
FE3
|
S:SF4401
|
2.7
|
8.7
|
1.0
|
FE2
|
S:SF4401
|
2.7
|
7.9
|
1.0
|
FE4
|
S:SF4401
|
2.7
|
8.3
|
1.0
|
CB
|
S:CYS215
|
3.5
|
8.1
|
1.0
|
N
|
S:LEU216
|
3.8
|
7.6
|
1.0
|
S1
|
S:SF4401
|
3.9
|
7.4
|
1.0
|
CA
|
S:CYS215
|
3.9
|
6.6
|
1.0
|
N
|
S:TYR217
|
4.2
|
8.7
|
1.0
|
C
|
S:CYS215
|
4.3
|
8.0
|
1.0
|
CB
|
S:PHE196
|
4.4
|
9.1
|
1.0
|
CD1
|
S:PHE196
|
4.4
|
10.1
|
1.0
|
ND1
|
S:HIS187
|
4.5
|
7.1
|
1.0
|
CB
|
S:TYR217
|
4.6
|
8.7
|
1.0
|
CE1
|
S:HIS187
|
4.7
|
10.4
|
1.0
|
CB
|
S:ARG192
|
4.7
|
7.8
|
1.0
|
O
|
S:ARG192
|
4.7
|
8.1
|
1.0
|
CG
|
S:PHE196
|
4.8
|
10.6
|
1.0
|
CA
|
S:LEU216
|
4.8
|
8.6
|
1.0
|
CA
|
S:TYR217
|
4.8
|
7.2
|
1.0
|
C
|
S:LEU216
|
4.8
|
7.3
|
1.0
|
SG
|
S:CYS221
|
4.9
|
8.3
|
1.0
|
SG
|
S:CYS190
|
4.9
|
8.0
|
1.0
|
|
Iron binding site 2 out
of 32 in 3use
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Iron Binding Sites List in 3use
Iron binding site 2 out
of 32 in the Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe401
b:7.9
occ:1.00
|
FE2
|
S:SF4401
|
0.0
|
7.9
|
1.0
|
S4
|
S:SF4401
|
2.3
|
8.3
|
1.0
|
S3
|
S:SF4401
|
2.3
|
8.3
|
1.0
|
SG
|
S:CYS190
|
2.3
|
8.0
|
1.0
|
S1
|
S:SF4401
|
2.3
|
7.4
|
1.0
|
FE3
|
S:SF4401
|
2.7
|
8.7
|
1.0
|
FE4
|
S:SF4401
|
2.7
|
8.3
|
1.0
|
FE1
|
S:SF4401
|
2.7
|
8.0
|
1.0
|
CB
|
S:CYS190
|
3.1
|
6.2
|
1.0
|
S2
|
S:SF4401
|
3.9
|
7.7
|
1.0
|
CB
|
S:ARG192
|
4.2
|
7.8
|
1.0
|
CD1
|
S:ILE243
|
4.2
|
7.8
|
1.0
|
CG2
|
S:ILE243
|
4.3
|
5.6
|
1.0
|
ND1
|
S:HIS187
|
4.5
|
7.1
|
1.0
|
CA
|
S:CYS190
|
4.6
|
7.1
|
1.0
|
C
|
S:ARG192
|
4.7
|
7.6
|
1.0
|
N
|
S:ARG192
|
4.7
|
7.7
|
1.0
|
CA
|
S:ARG192
|
4.7
|
6.7
|
1.0
|
SG
|
S:CYS221
|
4.8
|
8.3
|
1.0
|
N
|
S:ARG193
|
4.8
|
7.8
|
1.0
|
CG1
|
S:ILE243
|
4.8
|
6.6
|
1.0
|
SG
|
S:CYS215
|
4.9
|
8.8
|
1.0
|
C
|
S:CYS190
|
5.0
|
6.5
|
1.0
|
|
Iron binding site 3 out
of 32 in 3use
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Iron Binding Sites List in 3use
Iron binding site 3 out
of 32 in the Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe401
b:8.7
occ:1.00
|
FE3
|
S:SF4401
|
0.0
|
8.7
|
1.0
|
ND1
|
S:HIS187
|
2.1
|
7.1
|
1.0
|
S1
|
S:SF4401
|
2.3
|
7.4
|
1.0
|
S4
|
S:SF4401
|
2.3
|
8.3
|
1.0
|
S2
|
S:SF4401
|
2.3
|
7.7
|
1.0
|
FE2
|
S:SF4401
|
2.7
|
7.9
|
1.0
|
FE1
|
S:SF4401
|
2.7
|
8.0
|
1.0
|
FE4
|
S:SF4401
|
2.7
|
8.3
|
1.0
|
CE1
|
S:HIS187
|
2.8
|
10.4
|
1.0
|
CG
|
S:HIS187
|
3.2
|
9.6
|
1.0
|
CB
|
S:HIS187
|
3.8
|
7.2
|
1.0
|
S3
|
S:SF4401
|
3.9
|
8.3
|
1.0
|
NE2
|
S:HIS187
|
4.0
|
11.5
|
1.0
|
CA
|
S:HIS187
|
4.0
|
7.8
|
1.0
|
CD2
|
S:HIS187
|
4.2
|
11.1
|
1.0
|
CG
|
S:PRO224
|
4.2
|
9.7
|
1.0
|
CD
|
S:PRO224
|
4.3
|
8.5
|
1.0
|
CB
|
S:CYS190
|
4.5
|
6.2
|
1.0
|
SG
|
S:CYS190
|
4.7
|
8.0
|
1.0
|
SG
|
S:CYS215
|
4.7
|
8.8
|
1.0
|
CD1
|
S:PHE196
|
4.7
|
10.1
|
1.0
|
SG
|
S:CYS221
|
4.8
|
8.3
|
1.0
|
CD
|
S:ARG193
|
4.8
|
14.3
|
1.0
|
N
|
S:PRO224
|
4.8
|
8.5
|
1.0
|
O
|
S:HIS187
|
4.8
|
9.8
|
1.0
|
C
|
S:HIS187
|
5.0
|
9.1
|
1.0
|
N
|
S:HIS187
|
5.0
|
6.5
|
1.0
|
|
Iron binding site 4 out
of 32 in 3use
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Iron Binding Sites List in 3use
Iron binding site 4 out
of 32 in the Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe401
b:8.3
occ:1.00
|
FE4
|
S:SF4401
|
0.0
|
8.3
|
1.0
|
S2
|
S:SF4401
|
2.3
|
7.7
|
1.0
|
S1
|
S:SF4401
|
2.3
|
7.4
|
1.0
|
S3
|
S:SF4401
|
2.3
|
8.3
|
1.0
|
SG
|
S:CYS221
|
2.3
|
8.3
|
1.0
|
FE2
|
S:SF4401
|
2.7
|
7.9
|
1.0
|
FE3
|
S:SF4401
|
2.7
|
8.7
|
1.0
|
FE1
|
S:SF4401
|
2.7
|
8.0
|
1.0
|
CB
|
S:CYS221
|
3.2
|
6.3
|
1.0
|
S4
|
S:SF4401
|
3.9
|
8.3
|
1.0
|
CD1
|
S:ILE243
|
3.9
|
7.8
|
1.0
|
CG1
|
S:ILE243
|
4.4
|
6.6
|
1.0
|
CA
|
S:GLY223
|
4.5
|
7.2
|
1.0
|
CD
|
S:PRO224
|
4.5
|
8.5
|
1.0
|
N
|
S:GLY223
|
4.6
|
6.8
|
1.0
|
ND1
|
S:HIS187
|
4.6
|
7.1
|
1.0
|
CA
|
S:CYS221
|
4.6
|
6.7
|
1.0
|
SG
|
S:CYS215
|
4.7
|
8.8
|
1.0
|
SG
|
S:CYS190
|
4.7
|
8.0
|
1.0
|
N
|
S:TYR217
|
4.8
|
8.7
|
1.0
|
N
|
S:LEU216
|
4.8
|
7.6
|
1.0
|
C
|
S:CYS221
|
4.9
|
7.5
|
1.0
|
CB
|
S:LEU216
|
4.9
|
7.2
|
1.0
|
C
|
S:LEU216
|
5.0
|
7.3
|
1.0
|
|
Iron binding site 5 out
of 32 in 3use
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Iron Binding Sites List in 3use
Iron binding site 5 out
of 32 in the Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe402
b:7.6
occ:1.00
|
FE1
|
S:F3S402
|
0.0
|
7.6
|
1.0
|
S1
|
S:F3S402
|
2.2
|
6.9
|
1.0
|
S2
|
S:F3S402
|
2.2
|
7.3
|
1.0
|
S3
|
S:F3S402
|
2.2
|
6.9
|
1.0
|
SG
|
S:CYS252
|
2.3
|
7.2
|
1.0
|
FE4
|
S:F3S402
|
2.6
|
7.0
|
1.0
|
FE3
|
S:F3S402
|
2.7
|
7.2
|
1.0
|
CB
|
S:CYS252
|
3.4
|
6.7
|
1.0
|
O
|
L:HOH756
|
3.7
|
8.0
|
1.0
|
N
|
S:CYS252
|
3.8
|
6.9
|
1.0
|
S4
|
S:F3S402
|
3.9
|
8.0
|
1.0
|
O
|
S:HOH508
|
4.0
|
8.1
|
1.0
|
CA
|
S:CYS252
|
4.0
|
7.5
|
1.0
|
N
|
S:ALA253
|
4.5
|
7.3
|
1.0
|
C
|
S:CYS252
|
4.5
|
7.3
|
1.0
|
O
|
L:HOH740
|
4.5
|
11.1
|
1.0
|
ND2
|
S:ASN228
|
4.6
|
6.4
|
1.0
|
SG
|
S:CYS230
|
4.7
|
7.1
|
1.0
|
SG
|
S:CYS249
|
4.7
|
7.1
|
1.0
|
C
|
S:GLY251
|
5.0
|
6.9
|
1.0
|
CG
|
S:PRO242
|
5.0
|
5.8
|
1.0
|
|
Iron binding site 6 out
of 32 in 3use
Go back to
Iron Binding Sites List in 3use
Iron binding site 6 out
of 32 in the Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe402
b:7.2
occ:1.00
|
FE3
|
S:F3S402
|
0.0
|
7.2
|
1.0
|
S4
|
S:F3S402
|
2.2
|
8.0
|
1.0
|
S1
|
S:F3S402
|
2.2
|
6.9
|
1.0
|
S3
|
S:F3S402
|
2.2
|
6.9
|
1.0
|
SG
|
S:CYS230
|
2.3
|
7.1
|
1.0
|
FE1
|
S:F3S402
|
2.7
|
7.6
|
1.0
|
FE4
|
S:F3S402
|
2.7
|
7.0
|
1.0
|
CB
|
S:CYS230
|
3.2
|
5.0
|
1.0
|
S2
|
S:F3S402
|
3.9
|
7.3
|
1.0
|
ND2
|
S:ASN228
|
4.0
|
6.4
|
1.0
|
CD1
|
S:ILE186
|
4.2
|
8.3
|
1.0
|
O
|
S:HOH508
|
4.3
|
8.1
|
1.0
|
NE1
|
S:TRP235
|
4.3
|
8.0
|
1.0
|
CG
|
S:PRO242
|
4.5
|
5.8
|
1.0
|
CD
|
S:PRO242
|
4.5
|
5.5
|
1.0
|
CG
|
S:ASN228
|
4.6
|
6.4
|
1.0
|
CA
|
S:CYS230
|
4.7
|
5.5
|
1.0
|
CB
|
S:ASN228
|
4.7
|
6.6
|
1.0
|
SG
|
S:CYS252
|
4.7
|
7.2
|
1.0
|
CG1
|
S:ILE186
|
4.7
|
9.5
|
1.0
|
SG
|
S:CYS249
|
4.8
|
7.1
|
1.0
|
|
Iron binding site 7 out
of 32 in 3use
Go back to
Iron Binding Sites List in 3use
Iron binding site 7 out
of 32 in the Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe402
b:7.0
occ:1.00
|
FE4
|
S:F3S402
|
0.0
|
7.0
|
1.0
|
S4
|
S:F3S402
|
2.2
|
8.0
|
1.0
|
S2
|
S:F3S402
|
2.3
|
7.3
|
1.0
|
S3
|
S:F3S402
|
2.3
|
6.9
|
1.0
|
SG
|
S:CYS249
|
2.3
|
7.1
|
1.0
|
FE1
|
S:F3S402
|
2.6
|
7.6
|
1.0
|
FE3
|
S:F3S402
|
2.7
|
7.2
|
1.0
|
CB
|
S:CYS249
|
3.2
|
5.7
|
1.0
|
CA
|
S:CYS249
|
3.6
|
6.5
|
1.0
|
S1
|
S:F3S402
|
3.8
|
6.9
|
1.0
|
N
|
S:LEU250
|
4.0
|
6.2
|
1.0
|
N
|
S:GLY251
|
4.2
|
6.2
|
1.0
|
C
|
S:CYS249
|
4.3
|
6.0
|
1.0
|
N
|
S:CYS252
|
4.4
|
6.9
|
1.0
|
CG2
|
S:THR226
|
4.6
|
7.1
|
1.0
|
CG1
|
S:ILE186
|
4.6
|
9.5
|
1.0
|
CG
|
S:PRO242
|
4.7
|
5.8
|
1.0
|
SG
|
S:CYS252
|
4.7
|
7.2
|
1.0
|
CA
|
S:GLY251
|
4.8
|
7.1
|
1.0
|
SG
|
S:CYS230
|
4.8
|
7.1
|
1.0
|
N
|
S:CYS249
|
4.9
|
6.9
|
1.0
|
O
|
L:HOH740
|
5.0
|
11.1
|
1.0
|
CD1
|
S:ILE186
|
5.0
|
8.3
|
1.0
|
|
Iron binding site 8 out
of 32 in 3use
Go back to
Iron Binding Sites List in 3use
Iron binding site 8 out
of 32 in the Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe403
b:10.4
occ:0.50
|
FE1
|
S:F4S403
|
0.0
|
10.4
|
0.5
|
FE4
|
S:SF3404
|
0.0
|
10.4
|
0.5
|
S2
|
S:F4S403
|
2.3
|
8.9
|
0.5
|
S3
|
S:SF3404
|
2.3
|
8.9
|
0.5
|
S1
|
S:F4S403
|
2.3
|
8.4
|
0.5
|
S2
|
S:SF3404
|
2.3
|
8.4
|
0.5
|
SG
|
S:CYS17
|
2.3
|
8.4
|
1.0
|
SG
|
S:CYS19
|
2.4
|
8.5
|
1.0
|
FE2
|
S:F4S403
|
2.6
|
8.8
|
0.5
|
FE1
|
S:SF3404
|
2.6
|
8.8
|
0.5
|
FE4
|
S:F4S403
|
2.7
|
10.2
|
0.5
|
FE7
|
S:SF3404
|
3.2
|
10.7
|
0.5
|
CB
|
S:CYS19
|
3.5
|
7.3
|
1.0
|
CB
|
S:CYS17
|
3.5
|
5.9
|
1.0
|
FE3
|
S:F4S403
|
3.6
|
8.0
|
0.5
|
FE3
|
S:SF3404
|
3.6
|
8.0
|
0.5
|
N
|
S:CYS19
|
3.7
|
6.5
|
1.0
|
N
|
S:CYS17
|
3.7
|
8.1
|
1.0
|
S3
|
S:F4S403
|
3.7
|
8.3
|
0.5
|
S1
|
S:SF3404
|
3.7
|
8.3
|
0.5
|
CA
|
S:CYS17
|
4.0
|
6.6
|
1.0
|
N
|
S:THR18
|
4.1
|
7.6
|
1.0
|
CA
|
S:CYS19
|
4.1
|
7.3
|
1.0
|
NE2
|
L:HIS229
|
4.2
|
8.4
|
1.0
|
C
|
S:CYS17
|
4.2
|
8.1
|
1.0
|
SG
|
S:CYS149
|
4.4
|
6.8
|
1.0
|
O
|
S:HOH502
|
4.5
|
7.7
|
1.0
|
SG
|
S:CYS115
|
4.6
|
8.8
|
1.0
|
N
|
S:CYS20
|
4.7
|
7.2
|
1.0
|
CD2
|
L:HIS229
|
4.8
|
7.3
|
1.0
|
C
|
S:THR18
|
4.8
|
7.2
|
1.0
|
OE2
|
S:GLU76
|
4.9
|
13.0
|
0.5
|
C
|
S:GLU16
|
4.9
|
9.2
|
1.0
|
C
|
S:CYS19
|
4.9
|
7.1
|
1.0
|
SG
|
S:CYS20
|
5.0
|
8.7
|
1.0
|
CG
|
L:ARG74
|
5.0
|
5.8
|
1.0
|
|
Iron binding site 9 out
of 32 in 3use
Go back to
Iron Binding Sites List in 3use
Iron binding site 9 out
of 32 in the Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe403
b:8.8
occ:0.50
|
FE2
|
S:F4S403
|
0.0
|
8.8
|
0.5
|
FE1
|
S:SF3404
|
0.0
|
8.8
|
0.5
|
S3
|
S:F4S403
|
2.2
|
8.3
|
0.5
|
S1
|
S:SF3404
|
2.2
|
8.3
|
0.5
|
SG
|
S:CYS115
|
2.3
|
8.8
|
1.0
|
S1
|
S:F4S403
|
2.3
|
8.4
|
0.5
|
S2
|
S:SF3404
|
2.3
|
8.4
|
0.5
|
S2
|
S:F4S403
|
2.3
|
8.9
|
0.5
|
S3
|
S:SF3404
|
2.3
|
8.9
|
0.5
|
FE1
|
S:F4S403
|
2.6
|
10.4
|
0.5
|
FE4
|
S:SF3404
|
2.6
|
10.4
|
0.5
|
FE3
|
S:F4S403
|
2.7
|
8.0
|
0.5
|
FE3
|
S:SF3404
|
2.7
|
8.0
|
0.5
|
FE4
|
S:F4S403
|
3.0
|
10.2
|
0.5
|
CB
|
S:CYS115
|
3.3
|
6.4
|
1.0
|
FE7
|
S:SF3404
|
3.9
|
10.7
|
0.5
|
O
|
S:HOH520
|
3.9
|
8.6
|
1.0
|
N
|
S:CYS115
|
4.0
|
5.9
|
1.0
|
SG
|
S:CYS19
|
4.1
|
8.5
|
1.0
|
O
|
S:HOH502
|
4.2
|
7.7
|
1.0
|
CA
|
S:CYS115
|
4.2
|
6.6
|
1.0
|
SG
|
S:CYS120
|
4.3
|
8.3
|
1.0
|
CB
|
S:CYS120
|
4.4
|
6.6
|
1.0
|
N
|
S:CYS17
|
4.6
|
8.1
|
1.0
|
SG
|
S:CYS20
|
4.6
|
8.7
|
1.0
|
SG
|
S:CYS149
|
4.7
|
6.8
|
1.0
|
SG
|
S:CYS17
|
4.8
|
8.4
|
1.0
|
CA
|
S:GLU16
|
4.9
|
8.8
|
1.0
|
CB
|
S:GLU16
|
4.9
|
11.6
|
1.0
|
|
Iron binding site 10 out
of 32 in 3use
Go back to
Iron Binding Sites List in 3use
Iron binding site 10 out
of 32 in the Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Crystal Structure of E. Coli Hydrogenase-1 in Its As-Isolated Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe403
b:8.0
occ:0.50
|
FE3
|
S:F4S403
|
0.0
|
8.0
|
0.5
|
FE3
|
S:SF3404
|
0.0
|
8.0
|
0.5
|
SG
|
S:CYS149
|
2.3
|
6.8
|
1.0
|
S3
|
S:F4S403
|
2.3
|
8.3
|
0.5
|
S1
|
S:SF3404
|
2.3
|
8.3
|
0.5
|
S2
|
S:F4S403
|
2.3
|
8.9
|
0.5
|
S3
|
S:SF3404
|
2.3
|
8.9
|
0.5
|
SG
|
S:CYS120
|
2.3
|
8.3
|
1.0
|
FE2
|
S:F4S403
|
2.7
|
8.8
|
0.5
|
FE1
|
S:SF3404
|
2.7
|
8.8
|
0.5
|
CB
|
S:CYS149
|
3.3
|
6.7
|
1.0
|
CB
|
S:CYS120
|
3.4
|
6.6
|
1.0
|
FE1
|
S:F4S403
|
3.6
|
10.4
|
0.5
|
FE4
|
S:SF3404
|
3.6
|
10.4
|
0.5
|
CA
|
S:CYS149
|
4.0
|
5.7
|
1.0
|
SG
|
S:CYS115
|
4.0
|
8.8
|
1.0
|
FE4
|
S:F4S403
|
4.2
|
10.2
|
0.5
|
SG
|
S:CYS19
|
4.3
|
8.5
|
1.0
|
CG
|
L:ARG74
|
4.4
|
5.8
|
1.0
|
N
|
S:CYS115
|
4.5
|
5.9
|
1.0
|
CB
|
S:THR114
|
4.6
|
6.5
|
1.0
|
S1
|
S:F4S403
|
4.7
|
8.4
|
0.5
|
S2
|
S:SF3404
|
4.7
|
8.4
|
0.5
|
CA
|
S:CYS120
|
4.8
|
6.2
|
1.0
|
N
|
S:VAL121
|
4.9
|
6.8
|
1.0
|
C
|
S:CYS149
|
4.9
|
6.1
|
1.0
|
O
|
S:GLY148
|
4.9
|
6.2
|
1.0
|
N
|
S:THR114
|
5.0
|
6.4
|
1.0
|
|
Reference:
A.Volbeda,
P.Amara,
C.Darnault,
J.M.Mouesca,
A.Parkin,
M.M.Roessler,
F.A.Armstrong,
J.C.Fontecilla-Camps.
X-Ray Crystallographic and Computational Studies of the O2-Tolerant [Nife]-Hydrogenase 1 From Escherichia Coli. Proc.Natl.Acad.Sci.Usa V. 109 5305 2012.
ISSN: ISSN 0027-8424
PubMed: 22431599
DOI: 10.1073/PNAS.1119806109
Page generated: Sun Aug 4 21:17:12 2024
|