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Iron in PDB 4g39: 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: 4g39 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) 20.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 67.598, 77.045, 86.851, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 23.8

Other elements in 4g39:

The structure of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer also contains other interesting chemical elements:

Potassium (K) 2 atoms

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 4g39). 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: 4g39:
Jump to Iron binding site number: 1; 2; 3; 4; 5;

Iron binding site 1 out of 5 in 4g39

Go back to Iron Binding Sites List in 4g39
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:Fe604

b:29.1
occ:0.94
 FE1 A:SF4604 0.0 29.1 0.9
S3 A:SF4604 2.2 31.0 1.0
S2 A:SF4604 2.2 29.7 1.0
S4 A:SF4604 2.2 29.9 1.0
SG A:CYS434 2.2 23.7 1.0
FE4 A:SF4604 2.9 29.6 0.8
FE2 A:SF4604 3.0 29.5 0.8
CB A:CYS434 3.1 20.8 1.0
FE3 A:SF4604 3.1 28.4 0.8
N A:GLY478 3.5 20.7 1.0
S1 A:SF4604 3.8 30.3 1.0
N A:SER436 3.8 26.6 1.0
CA A:GLY478 3.8 20.9 1.0
CA A:SER436 4.2 31.9 1.0
OG1 A:THR477 4.3 24.3 1.0
N A:CYS479 4.3 26.4 1.0
CA A:CYS434 4.4 25.9 1.0
N A:VAL435 4.4 26.2 1.0
CB A:SER436 4.4 25.4 1.0
CB A:CYS483 4.5 23.9 1.0
C A:CYS434 4.5 28.9 1.0
C A:GLY478 4.5 23.0 1.0
C A:THR477 4.6 20.9 1.0
SG A:CYS483 4.7 26.4 1.0
C A:VAL435 4.8 25.7 1.0
CA A:THR477 4.9 20.2 1.0
OG A:SER436 4.9 26.8 1.0

Iron binding site 2 out of 5 in 4g39

Go back to Iron Binding Sites List in 4g39
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:Fe604

b:29.5
occ:0.83
 FE2 A:SF4604 0.0 29.5 0.8
S3 A:SF4604 2.2 31.0 1.0
S4 A:SF4604 2.2 29.9 1.0
S1 A:SF4604 2.2 30.3 1.0
SG A:CYS440 2.2 24.8 1.0
FE3 A:SF4604 3.0 28.4 0.8
FE1 A:SF4604 3.0 29.1 0.9
FE4 A:SF4604 3.0 29.6 0.8
CB A:CYS440 3.2 30.9 1.0
S2 A:SF4604 3.8 29.7 1.0
N A:SER436 4.3 26.6 1.0
CA A:SER436 4.3 31.9 1.0
CBA A:SRM605 4.4 29.8 1.0
N A:ALA443 4.4 31.4 1.0
C3A A:SRM605 4.5 30.9 1.0
CA A:ALA443 4.6 30.3 1.0
CA A:CYS440 4.6 25.1 1.0
CB A:LEU442 4.6 31.3 1.0
CDA A:SRM605 4.6 33.0 1.0
C A:LEU442 4.7 29.8 1.0
CB A:ALA443 4.7 23.9 1.0
SG A:CYS479 4.8 26.6 1.0
C4A A:SRM605 4.8 31.5 1.0
N A:LEU442 5.0 25.1 1.0
CA A:LEU442 5.0 29.9 1.0

Iron binding site 3 out of 5 in 4g39

Go back to Iron Binding Sites List in 4g39
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:Fe604

b:28.4
occ:0.81
 FE3 A:SF4604 0.0 28.4 0.8
S2 A:SF4604 2.2 29.7 1.0
S4 A:SF4604 2.2 29.9 1.0
S1 A:SF4604 2.2 30.3 1.0
SG A:CYS479 2.2 26.6 1.0
FE2 A:SF4604 3.0 29.5 0.8
FE4 A:SF4604 3.1 29.6 0.8
FE1 A:SF4604 3.1 29.1 0.9
CB A:CYS479 3.2 22.2 1.0
N A:CYS479 3.4 26.4 1.0
CA A:CYS479 3.7 21.4 1.0
S3 A:SF4604 3.9 31.0 1.0
O A:CYS479 3.9 20.9 1.0
C A:CYS479 4.0 22.6 1.0
CB A:ASN481 4.1 25.1 1.0
C A:GLY478 4.1 23.0 1.0
ND2 A:ASN481 4.2 26.3 1.0
N A:ASN481 4.5 27.1 1.0
CA A:GLY478 4.6 20.9 1.0
O A:LEU442 4.6 29.4 1.0
CG A:ASN481 4.6 33.0 1.0
N A:GLY478 4.7 20.7 1.0
SG A:CYS483 4.8 26.4 1.0
CA A:ASN481 4.8 25.2 1.0
SG A:CYS440 4.9 24.8 1.0
C A:LEU442 4.9 29.8 1.0
CB A:LEU442 4.9 31.3 1.0
O A:GLY478 4.9 24.7 1.0
N A:PRO480 4.9 24.3 1.0
CA A:ALA443 4.9 30.3 1.0
N A:GLY482 5.0 24.1 1.0

Iron binding site 4 out of 5 in 4g39

Go back to Iron Binding Sites List in 4g39
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:Fe604

b:29.6
occ:0.78
 FE4 A:SF4604 0.0 29.6 0.8
SG A:CYS483 2.1 26.4 1.0
S1 A:SF4604 2.2 30.3 1.0
S3 A:SF4604 2.2 31.0 1.0
S2 A:SF4604 2.2 29.7 1.0
FE1 A:SF4604 2.9 29.1 0.9
CB A:CYS483 3.0 23.9 1.0
FE2 A:SF4604 3.0 29.5 0.8
FE3 A:SF4604 3.1 28.4 0.8
NA A:SRM605 3.6 30.7 0.8
S4 A:SF4604 3.8 29.9 1.0
C4A A:SRM605 3.8 31.5 1.0
FE A:SRM605 4.1 34.4 1.0
C1A A:SRM605 4.1 32.5 0.8
N A:CYS483 4.1 21.5 1.0
CA A:CYS483 4.1 24.0 1.0
CHB A:SRM605 4.2 30.9 1.0
ND A:SRM605 4.3 30.3 0.9
C3A A:SRM605 4.3 30.9 1.0
CB A:ASN481 4.5 25.1 1.0
C4D A:SRM605 4.5 32.9 0.8
CB A:CYS434 4.5 20.8 1.0
CHA A:SRM605 4.5 30.7 1.0
C1B A:SRM605 4.6 24.6 1.0
NB A:SRM605 4.6 29.6 0.6
SG A:CYS434 4.7 23.7 1.0
C2A A:SRM605 4.8 32.8 1.0
SG A:CYS440 4.8 24.8 1.0
C1D A:SRM605 4.9 32.0 1.0
SG A:CYS479 5.0 26.6 1.0

Iron binding site 5 out of 5 in 4g39

Go back to Iron Binding Sites List in 4g39
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:Fe605

b:34.4
occ:1.00
 FE A:SRM605 0.0 34.4 1.0
NB A:SRM605 1.9 29.6 0.6
NA A:SRM605 2.0 30.7 0.8
NC A:SRM605 2.0 27.1 0.7
ND A:SRM605 2.0 30.3 0.9
SG A:CYS483 2.4 26.4 1.0
O3 A:PO4601 2.7 37.6 0.9
C4B A:SRM605 3.0 30.4 1.0
C4A A:SRM605 3.0 31.5 1.0
C1B A:SRM605 3.0 24.6 1.0
C1D A:SRM605 3.0 32.0 1.0
C4C A:SRM605 3.0 27.5 1.0
C1C A:SRM605 3.0 28.7 0.9
C1A A:SRM605 3.0 32.5 0.8
C4D A:SRM605 3.0 32.9 0.8
CHB A:SRM605 3.3 30.9 1.0
CHD A:SRM605 3.3 29.3 1.0
CHC A:SRM605 3.4 25.2 1.0
CB A:CYS483 3.4 23.9 1.0
CHA A:SRM605 3.4 30.7 1.0
P A:PO4601 4.0 48.9 0.9
FE4 A:SF4604 4.1 29.6 0.8
O4 A:PO4601 4.2 41.9 0.8
C3B A:SRM605 4.2 27.4 1.0
C2B A:SRM605 4.2 28.7 0.3
C3A A:SRM605 4.2 30.9 1.0
CA A:CYS483 4.2 24.0 1.0
C2A A:SRM605 4.3 32.8 1.0
C3C A:SRM605 4.3 27.6 1.0
C2D A:SRM605 4.3 34.2 0.9
C2C A:SRM605 4.3 27.6 0.9
C3D A:SRM605 4.3 30.2 1.0
NZ A:LYS215 4.7 38.5 1.0
CMA A:SRM605 4.8 33.4 1.0
CAB A:SRM605 4.8 29.9 1.0
CDB A:SRM605 4.8 28.7 0.8
O2 A:PO4601 4.9 38.2 0.7
O1 A:PO4601 4.9 45.5 1.0
N A:CYS483 5.0 21.5 1.0
NH2 A:ARG83 5.0 32.8 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 02:36:12 2024

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