Iron in PDB 4g38: Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer
Enzymatic activity of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer
All present enzymatic activity of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer:
1.8.1.2;
Protein crystallography data
The structure of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer, PDB code: 4g38
was solved by
K.W.Smith,
M.E.Stroupe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
22.77 /
1.56
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
66.327,
76.171,
81.463,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
14 /
17.8
|
Other elements in 4g38:
The structure of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer
(pdb code 4g38). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 5 binding sites of Iron where determined in the
Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer, PDB code: 4g38:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
Iron binding site 1 out
of 5 in 4g38
Go back to
Iron Binding Sites List in 4g38
Iron binding site 1 out
of 5 in the Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe603
b:10.4
occ:1.00
|
FE1
|
A:SF4603
|
0.0
|
10.4
|
1.0
|
S4
|
A:SF4603
|
2.2
|
9.9
|
1.0
|
S3
|
A:SF4603
|
2.2
|
10.2
|
1.0
|
S2
|
A:SF4603
|
2.2
|
10.0
|
1.0
|
SG
|
A:CYS434
|
2.3
|
8.7
|
1.0
|
FE4
|
A:SF4603
|
2.6
|
11.3
|
1.0
|
FE2
|
A:SF4603
|
2.7
|
11.0
|
1.0
|
FE3
|
A:SF4603
|
2.7
|
10.7
|
1.0
|
CB
|
A:CYS434
|
3.3
|
7.6
|
1.0
|
N
|
A:GLY478
|
3.6
|
8.7
|
1.0
|
S1
|
A:SF4603
|
3.7
|
10.2
|
1.0
|
N
|
A:SER436
|
4.0
|
10.2
|
1.0
|
CA
|
A:GLY478
|
4.0
|
9.4
|
1.0
|
CA
|
A:SER436
|
4.2
|
9.6
|
1.0
|
N
|
A:CYS479
|
4.3
|
8.4
|
1.0
|
OG1
|
A:THR477
|
4.3
|
11.3
|
1.0
|
CB
|
A:CYS483
|
4.4
|
8.1
|
1.0
|
SG
|
A:CYS483
|
4.4
|
9.2
|
1.0
|
CB
|
A:SER436
|
4.4
|
10.2
|
1.0
|
C
|
A:GLY478
|
4.5
|
8.9
|
1.0
|
CA
|
A:CYS434
|
4.7
|
8.1
|
1.0
|
C
|
A:THR477
|
4.8
|
9.0
|
1.0
|
N
|
A:VAL435
|
4.8
|
10.2
|
1.0
|
C
|
A:CYS434
|
4.8
|
8.9
|
1.0
|
SG
|
A:CYS440
|
4.9
|
10.8
|
1.0
|
SG
|
A:CYS479
|
4.9
|
10.3
|
1.0
|
|
Iron binding site 2 out
of 5 in 4g38
Go back to
Iron Binding Sites List in 4g38
Iron binding site 2 out
of 5 in the Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe603
b:11.0
occ:1.00
|
FE2
|
A:SF4603
|
0.0
|
11.0
|
1.0
|
S3
|
A:SF4603
|
2.2
|
10.2
|
1.0
|
S4
|
A:SF4603
|
2.2
|
9.9
|
1.0
|
S1
|
A:SF4603
|
2.2
|
10.2
|
1.0
|
SG
|
A:CYS440
|
2.3
|
10.8
|
1.0
|
FE1
|
A:SF4603
|
2.7
|
10.4
|
1.0
|
FE4
|
A:SF4603
|
2.7
|
11.3
|
1.0
|
FE3
|
A:SF4603
|
2.7
|
10.7
|
1.0
|
CB
|
A:CYS440
|
3.3
|
11.0
|
1.0
|
S2
|
A:SF4603
|
3.8
|
10.0
|
1.0
|
CA
|
A:SER436
|
4.3
|
9.6
|
1.0
|
C3A
|
A:SRM604
|
4.4
|
12.2
|
1.0
|
N
|
A:SER436
|
4.4
|
10.2
|
1.0
|
N
|
A:ALA443
|
4.5
|
12.2
|
1.0
|
CBA
|
A:SRM604
|
4.5
|
12.4
|
1.0
|
CB
|
A:LEU442
|
4.6
|
12.4
|
1.0
|
CA
|
A:CYS440
|
4.7
|
11.1
|
1.0
|
SG
|
A:CYS479
|
4.7
|
10.3
|
1.0
|
CDA
|
A:SRM604
|
4.7
|
14.4
|
1.0
|
CA
|
A:ALA443
|
4.7
|
11.6
|
1.0
|
C4A
|
A:SRM604
|
4.8
|
11.3
|
1.0
|
SG
|
A:CYS434
|
4.8
|
8.7
|
1.0
|
C
|
A:LEU442
|
4.8
|
12.6
|
1.0
|
SG
|
A:CYS483
|
4.8
|
9.2
|
1.0
|
CB
|
A:ALA443
|
4.9
|
12.5
|
1.0
|
|
Iron binding site 3 out
of 5 in 4g38
Go back to
Iron Binding Sites List in 4g38
Iron binding site 3 out
of 5 in the Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe603
b:10.7
occ:1.00
|
FE3
|
A:SF4603
|
0.0
|
10.7
|
1.0
|
S2
|
A:SF4603
|
2.2
|
10.0
|
1.0
|
S4
|
A:SF4603
|
2.2
|
9.9
|
1.0
|
S1
|
A:SF4603
|
2.2
|
10.2
|
1.0
|
SG
|
A:CYS479
|
2.3
|
10.3
|
1.0
|
FE2
|
A:SF4603
|
2.7
|
11.0
|
1.0
|
FE1
|
A:SF4603
|
2.7
|
10.4
|
1.0
|
FE4
|
A:SF4603
|
2.7
|
11.3
|
1.0
|
CB
|
A:CYS479
|
3.3
|
10.0
|
1.0
|
N
|
A:CYS479
|
3.5
|
8.4
|
1.0
|
S3
|
A:SF4603
|
3.8
|
10.2
|
1.0
|
CA
|
A:CYS479
|
3.8
|
8.9
|
1.0
|
O
|
A:CYS479
|
4.1
|
8.8
|
1.0
|
C
|
A:CYS479
|
4.1
|
9.0
|
1.0
|
CB
|
A:ASN481
|
4.2
|
9.6
|
1.0
|
C
|
A:GLY478
|
4.2
|
8.9
|
1.0
|
ND2
|
A:ASN481
|
4.3
|
12.5
|
1.0
|
SG
|
A:CYS440
|
4.6
|
10.8
|
1.0
|
CA
|
A:GLY478
|
4.6
|
9.4
|
1.0
|
SG
|
A:CYS483
|
4.6
|
9.2
|
1.0
|
N
|
A:GLY478
|
4.7
|
8.7
|
1.0
|
N
|
A:ASN481
|
4.7
|
8.6
|
1.0
|
CB
|
A:LEU442
|
4.7
|
12.4
|
1.0
|
O
|
A:LEU442
|
4.8
|
14.2
|
1.0
|
CG
|
A:ASN481
|
4.8
|
11.1
|
1.0
|
C
|
A:LEU442
|
4.8
|
12.6
|
1.0
|
CA
|
A:ALA443
|
4.9
|
11.6
|
1.0
|
O
|
A:GLY478
|
4.9
|
9.5
|
1.0
|
SG
|
A:CYS434
|
4.9
|
8.7
|
1.0
|
N
|
A:GLY482
|
4.9
|
8.8
|
1.0
|
CA
|
A:ASN481
|
4.9
|
8.8
|
1.0
|
N
|
A:ALA443
|
5.0
|
12.2
|
1.0
|
|
Iron binding site 4 out
of 5 in 4g38
Go back to
Iron Binding Sites List in 4g38
Iron binding site 4 out
of 5 in the Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe603
b:11.3
occ:1.00
|
FE4
|
A:SF4603
|
0.0
|
11.3
|
1.0
|
S1
|
A:SF4603
|
2.2
|
10.2
|
1.0
|
S3
|
A:SF4603
|
2.2
|
10.2
|
1.0
|
SG
|
A:CYS483
|
2.2
|
9.2
|
1.0
|
S2
|
A:SF4603
|
2.2
|
10.0
|
1.0
|
FE1
|
A:SF4603
|
2.6
|
10.4
|
1.0
|
FE2
|
A:SF4603
|
2.7
|
11.0
|
1.0
|
FE3
|
A:SF4603
|
2.7
|
10.7
|
1.0
|
CB
|
A:CYS483
|
3.1
|
8.1
|
1.0
|
S4
|
A:SF4603
|
3.7
|
9.9
|
1.0
|
NA
|
A:SRM604
|
4.0
|
11.3
|
1.0
|
C4A
|
A:SRM604
|
4.0
|
11.3
|
1.0
|
N
|
A:CYS483
|
4.1
|
8.2
|
1.0
|
CA
|
A:CYS483
|
4.3
|
7.9
|
1.0
|
C1A
|
A:SRM604
|
4.3
|
11.9
|
1.0
|
FE
|
A:SRM604
|
4.4
|
10.9
|
1.0
|
CHB
|
A:SRM604
|
4.4
|
10.6
|
1.0
|
CB
|
A:ASN481
|
4.5
|
9.6
|
1.0
|
SG
|
A:CYS434
|
4.5
|
8.7
|
1.0
|
C3A
|
A:SRM604
|
4.5
|
12.2
|
1.0
|
ND
|
A:SRM604
|
4.6
|
11.8
|
1.0
|
CB
|
A:CYS434
|
4.6
|
7.6
|
1.0
|
C4D
|
A:SRM604
|
4.7
|
11.8
|
1.0
|
SG
|
A:CYS440
|
4.7
|
10.8
|
1.0
|
SG
|
A:CYS479
|
4.7
|
10.3
|
1.0
|
CHA
|
A:SRM604
|
4.7
|
11.8
|
1.0
|
C1B
|
A:SRM604
|
4.8
|
11.0
|
1.0
|
NB
|
A:SRM604
|
4.8
|
10.9
|
1.0
|
N
|
A:GLY482
|
4.9
|
8.8
|
1.0
|
|
Iron binding site 5 out
of 5 in 4g38
Go back to
Iron Binding Sites List in 4g38
Iron binding site 5 out
of 5 in the Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe604
b:10.9
occ:1.00
|
FE
|
A:SRM604
|
0.0
|
10.9
|
1.0
|
NC
|
A:SRM604
|
2.0
|
10.5
|
1.0
|
NB
|
A:SRM604
|
2.0
|
10.9
|
1.0
|
ND
|
A:SRM604
|
2.0
|
11.8
|
1.0
|
NA
|
A:SRM604
|
2.0
|
11.3
|
1.0
|
O1
|
A:PO4601
|
2.1
|
11.8
|
1.0
|
SG
|
A:CYS483
|
2.7
|
9.2
|
1.0
|
C1D
|
A:SRM604
|
3.0
|
11.2
|
1.0
|
C4A
|
A:SRM604
|
3.0
|
11.3
|
1.0
|
C1C
|
A:SRM604
|
3.0
|
9.6
|
1.0
|
C4B
|
A:SRM604
|
3.0
|
10.6
|
1.0
|
C4C
|
A:SRM604
|
3.0
|
10.7
|
1.0
|
C4D
|
A:SRM604
|
3.0
|
11.8
|
1.0
|
C1B
|
A:SRM604
|
3.0
|
11.0
|
1.0
|
C1A
|
A:SRM604
|
3.0
|
11.9
|
1.0
|
P
|
A:PO4601
|
3.3
|
11.5
|
1.0
|
CHD
|
A:SRM604
|
3.4
|
10.8
|
1.0
|
CHB
|
A:SRM604
|
3.4
|
10.6
|
1.0
|
CHC
|
A:SRM604
|
3.4
|
10.1
|
1.0
|
CHA
|
A:SRM604
|
3.4
|
11.8
|
1.0
|
O3
|
A:PO4601
|
3.5
|
12.5
|
1.0
|
CB
|
A:CYS483
|
3.7
|
8.1
|
1.0
|
O2
|
A:PO4601
|
4.2
|
11.8
|
1.0
|
C3B
|
A:SRM604
|
4.2
|
10.6
|
1.0
|
NH2
|
A:ARG83
|
4.3
|
12.4
|
0.4
|
C2C
|
A:SRM604
|
4.3
|
10.3
|
1.0
|
C3D
|
A:SRM604
|
4.3
|
12.7
|
1.0
|
C2D
|
A:SRM604
|
4.3
|
11.7
|
1.0
|
C3C
|
A:SRM604
|
4.3
|
10.8
|
1.0
|
C3A
|
A:SRM604
|
4.3
|
12.2
|
1.0
|
C2B
|
A:SRM604
|
4.3
|
10.5
|
1.0
|
C2A
|
A:SRM604
|
4.3
|
12.6
|
1.0
|
O4
|
A:PO4601
|
4.4
|
13.0
|
1.0
|
FE4
|
A:SF4603
|
4.4
|
11.3
|
1.0
|
NZ
|
A:LYS215
|
4.5
|
19.0
|
1.0
|
CA
|
A:CYS483
|
4.6
|
7.9
|
1.0
|
NZ
|
A:LYS217
|
4.8
|
9.9
|
1.0
|
CAB
|
A:SRM604
|
4.8
|
9.9
|
1.0
|
NH1
|
A:ARG83
|
4.8
|
15.6
|
0.6
|
CMA
|
A:SRM604
|
4.9
|
13.9
|
1.0
|
|
Reference:
K.W.Smith,
M.E.Stroupe.
Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer. Biochemistry V. 51 9857 2012.
ISSN: ISSN 0006-2960
PubMed: 23153334
DOI: 10.1021/BI300947A
Page generated: Mon Aug 5 02:33:28 2024
|