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Iron in PDB 1mg2: Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin

Enzymatic activity of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin

All present enzymatic activity of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin:
1.4.99.3;

Protein crystallography data

The structure of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin, PDB code: 1mg2 was solved by D.Sun, Z.W.Chen, F.S.Mathews, V.L.Davidson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 79.122, 188.201, 127.100, 90.00, 99.24, 90.00
R / Rfree (%) 17.3 / 21

Other elements in 1mg2:

The structure of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin also contains other interesting chemical elements:

Copper (Cu) 4 atoms
Sodium (Na) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin (pdb code 1mg2). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin, PDB code: 1mg2:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1mg2

Go back to Iron Binding Sites List in 1mg2
Iron binding site 1 out of 4 in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe200

b:16.0
occ:1.00
FE D:HEM200 0.0 16.0 1.0
ND D:HEM200 2.0 11.8 1.0
NC D:HEM200 2.0 12.1 1.0
NE2 D:HIS61 2.0 16.7 1.0
NB D:HEM200 2.0 11.3 1.0
NA D:HEM200 2.0 10.7 1.0
SD D:MET101 2.3 16.1 1.0
CE1 D:HIS61 3.0 13.0 1.0
C4D D:HEM200 3.0 14.4 1.0
C1C D:HEM200 3.0 17.7 1.0
C1D D:HEM200 3.0 13.5 1.0
C4C D:HEM200 3.0 14.7 1.0
C1A D:HEM200 3.0 11.4 1.0
C1B D:HEM200 3.0 12.5 1.0
C4B D:HEM200 3.1 14.3 1.0
C4A D:HEM200 3.1 12.2 1.0
CD2 D:HIS61 3.1 14.6 1.0
CHA D:HEM200 3.4 13.2 1.0
CHD D:HEM200 3.4 14.0 1.0
CHB D:HEM200 3.4 9.2 1.0
CHC D:HEM200 3.4 15.8 1.0
CE D:MET101 3.5 11.9 1.0
CG D:MET101 3.5 15.9 1.0
CG D:HIS61 4.1 15.8 1.0
ND1 D:HIS61 4.2 18.7 1.0
CB D:MET101 4.2 19.1 1.0
C3D D:HEM200 4.3 15.7 1.0
C2D D:HEM200 4.3 15.9 1.0
C3C D:HEM200 4.3 17.7 1.0
C2C D:HEM200 4.3 19.0 1.0
C3B D:HEM200 4.3 14.2 1.0
C2B D:HEM200 4.3 11.9 1.0
C2A D:HEM200 4.3 13.6 1.0
C3A D:HEM200 4.3 11.7 1.0

Iron binding site 2 out of 4 in 1mg2

Go back to Iron Binding Sites List in 1mg2
Iron binding site 2 out of 4 in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Fe200

b:18.2
occ:1.00
FE H:HEM200 0.0 18.2 1.0
ND H:HEM200 2.0 19.7 1.0
NC H:HEM200 2.0 18.6 1.0
NE2 H:HIS61 2.0 12.8 1.0
NB H:HEM200 2.0 18.3 1.0
NA H:HEM200 2.0 20.2 1.0
SD H:MET101 2.2 21.2 1.0
C4D H:HEM200 3.0 19.2 1.0
C1D H:HEM200 3.0 20.6 1.0
CE1 H:HIS61 3.0 14.4 1.0
C1C H:HEM200 3.0 20.6 1.0
C4C H:HEM200 3.0 20.6 1.0
C1A H:HEM200 3.0 18.8 1.0
C1B H:HEM200 3.1 18.9 1.0
C4A H:HEM200 3.1 18.7 1.0
C4B H:HEM200 3.1 17.8 1.0
CD2 H:HIS61 3.1 11.3 1.0
CHA H:HEM200 3.4 19.7 1.0
CHD H:HEM200 3.4 19.4 1.0
CHB H:HEM200 3.4 18.2 1.0
CHC H:HEM200 3.4 21.3 1.0
CE H:MET101 3.4 20.6 1.0
CG H:MET101 3.5 24.0 1.0
CG H:HIS61 4.1 13.2 1.0
CB H:MET101 4.1 25.1 1.0
ND1 H:HIS61 4.2 15.6 1.0
C3D H:HEM200 4.3 21.0 1.0
C2D H:HEM200 4.3 21.2 1.0
C3C H:HEM200 4.3 22.5 1.0
C2C H:HEM200 4.3 21.0 1.0
C3B H:HEM200 4.3 17.4 1.0
C2A H:HEM200 4.3 20.2 1.0
C2B H:HEM200 4.3 16.5 1.0
C3A H:HEM200 4.3 19.9 1.0
CA H:MET101 4.8 24.8 1.0

Iron binding site 3 out of 4 in 1mg2

Go back to Iron Binding Sites List in 1mg2
Iron binding site 3 out of 4 in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Fe200

b:17.1
occ:1.00
FE L:HEM200 0.0 17.1 1.0
ND L:HEM200 2.0 17.1 1.0
NC L:HEM200 2.0 21.5 1.0
NB L:HEM200 2.0 18.2 1.0
NA L:HEM200 2.0 18.4 1.0
NE2 L:HIS61 2.0 14.1 1.0
SD L:MET101 2.2 17.0 1.0
C4D L:HEM200 3.0 17.6 1.0
C1C L:HEM200 3.0 22.9 1.0
C1B L:HEM200 3.0 16.9 1.0
C1D L:HEM200 3.0 18.4 1.0
C4C L:HEM200 3.1 20.2 1.0
C1A L:HEM200 3.1 16.9 1.0
C4B L:HEM200 3.1 19.2 1.0
C4A L:HEM200 3.1 17.8 1.0
CE1 L:HIS61 3.1 15.1 1.0
CD2 L:HIS61 3.1 15.2 1.0
CHA L:HEM200 3.4 15.4 1.0
CHD L:HEM200 3.4 18.3 1.0
CHB L:HEM200 3.4 16.8 1.0
CHC L:HEM200 3.4 21.2 1.0
CE L:MET101 3.5 11.6 1.0
CG L:MET101 3.6 17.0 1.0
CG L:HIS61 4.1 14.2 1.0
CB L:MET101 4.2 21.1 1.0
ND1 L:HIS61 4.3 19.2 1.0
C3D L:HEM200 4.3 17.3 1.0
C2D L:HEM200 4.3 18.6 1.0
C3B L:HEM200 4.3 19.1 1.0
C3C L:HEM200 4.3 21.4 1.0
C2B L:HEM200 4.3 19.3 1.0
C2C L:HEM200 4.3 22.9 1.0
C2A L:HEM200 4.3 18.0 1.0
C3A L:HEM200 4.3 19.2 1.0
CA L:MET101 4.8 20.8 1.0

Iron binding site 4 out of 4 in 1mg2

Go back to Iron Binding Sites List in 1mg2
Iron binding site 4 out of 4 in the Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
P:Fe200

b:22.9
occ:1.00
FE P:HEM200 0.0 22.9 1.0
ND P:HEM200 2.0 24.7 1.0
NE2 P:HIS61 2.0 18.8 1.0
NC P:HEM200 2.0 25.1 1.0
NB P:HEM200 2.0 27.9 1.0
NA P:HEM200 2.0 18.9 1.0
SD P:MET101 2.3 29.2 1.0
CE1 P:HIS61 3.0 23.2 1.0
C4D P:HEM200 3.0 25.7 1.0
C1C P:HEM200 3.0 29.7 1.0
C1D P:HEM200 3.0 25.9 1.0
C1A P:HEM200 3.0 20.9 1.0
C1B P:HEM200 3.0 26.6 1.0
C4C P:HEM200 3.1 27.5 1.0
C4A P:HEM200 3.1 20.4 1.0
C4B P:HEM200 3.1 28.1 1.0
CD2 P:HIS61 3.1 20.5 1.0
CHA P:HEM200 3.4 23.6 1.0
CHD P:HEM200 3.4 27.2 1.0
CHB P:HEM200 3.4 24.1 1.0
CHC P:HEM200 3.4 30.4 1.0
CE P:MET101 3.5 29.8 1.0
CG P:MET101 3.6 29.2 1.0
CG P:HIS61 4.1 20.5 1.0
ND1 P:HIS61 4.2 22.6 1.0
C3D P:HEM200 4.3 25.4 1.0
C2D P:HEM200 4.3 28.7 1.0
C2A P:HEM200 4.3 21.1 1.0
C3A P:HEM200 4.3 20.6 1.0
C2B P:HEM200 4.3 26.5 1.0
C3B P:HEM200 4.3 26.6 1.0
C3C P:HEM200 4.3 29.1 1.0
C2C P:HEM200 4.3 28.4 1.0
CB P:MET101 4.3 29.1 1.0

Reference:

D.Sun, Z.W.Chen, F.S.Mathews, V.L.Davidson. Mutation of Alpha PHE55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling For Its Electron Transfer Reaction with Amicyanin Biochemistry V. 41 13926 2002.
ISSN: ISSN 0006-2960
PubMed: 12437349
DOI: 10.1021/BI026654X
Page generated: Sun Dec 13 14:23:36 2020

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