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Iron in PDB 2zon: Crystal Structure of Electron Transfer Complex of Nitrite Reductase with Cytochrome C

Enzymatic activity of Crystal Structure of Electron Transfer Complex of Nitrite Reductase with Cytochrome C

All present enzymatic activity of Crystal Structure of Electron Transfer Complex of Nitrite Reductase with Cytochrome C:
1.7.2.1;

Protein crystallography data

The structure of Crystal Structure of Electron Transfer Complex of Nitrite Reductase with Cytochrome C, PDB code: 2zon was solved by M.Nojiri, H.Koteishi, K.Yamaguchi, S.Suzuki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.345, 103.942, 163.144, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 19.5

Other elements in 2zon:

The structure of Crystal Structure of Electron Transfer Complex of Nitrite Reductase with Cytochrome C also contains other interesting chemical elements:

Copper (Cu) 6 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Electron Transfer Complex of Nitrite Reductase with Cytochrome C (pdb code 2zon). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Electron Transfer Complex of Nitrite Reductase with Cytochrome C, PDB code: 2zon:

Iron binding site 1 out of 1 in 2zon

Go back to Iron Binding Sites List in 2zon
Iron binding site 1 out of 1 in the Crystal Structure of Electron Transfer Complex of Nitrite Reductase with Cytochrome C


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 Electron Transfer Complex of Nitrite Reductase with Cytochrome C within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe200

b:19.4
occ:1.00
FE G:HEM200 0.0 19.4 1.0
NE2 G:HIS24 2.1 18.7 1.0
NA G:HEM200 2.1 17.9 1.0
ND G:HEM200 2.1 19.3 1.0
NB G:HEM200 2.1 16.9 1.0
NC G:HEM200 2.1 18.8 1.0
SD G:MET62 2.4 20.6 1.0
CE1 G:HIS24 3.0 19.0 1.0
C4A G:HEM200 3.0 19.3 1.0
C1A G:HEM200 3.1 20.6 1.0
C4D G:HEM200 3.1 20.4 1.0
C1D G:HEM200 3.1 20.2 1.0
C1B G:HEM200 3.1 19.6 1.0
C4B G:HEM200 3.1 18.9 1.0
CD2 G:HIS24 3.1 20.2 1.0
C1C G:HEM200 3.1 19.1 1.0
C4C G:HEM200 3.1 20.8 1.0
CHA G:HEM200 3.4 19.6 1.0
CHB G:HEM200 3.4 19.7 1.0
CHD G:HEM200 3.4 21.1 1.0
CHC G:HEM200 3.4 19.5 1.0
CG G:MET62 3.5 21.4 1.0
CE G:MET62 3.6 20.4 1.0
CB G:MET62 4.0 21.9 1.0
ND1 G:HIS24 4.1 19.0 1.0
CG G:HIS24 4.2 20.4 1.0
C3A G:HEM200 4.2 19.2 1.0
C2D G:HEM200 4.2 20.6 1.0
C2A G:HEM200 4.2 19.8 1.0
C3D G:HEM200 4.3 21.0 1.0
C2B G:HEM200 4.3 17.4 1.0
C3B G:HEM200 4.3 17.9 1.0
C2C G:HEM200 4.3 19.9 1.0
C3C G:HEM200 4.3 19.5 1.0

Reference:

M.Nojiri, H.Koteishi, T.Nakagami, K.Kobayashi, T.Inoue, K.Yamaguchi, S.Suzuki. Structural Basis of Inter-Protein Electron Transfer For Nitrite Reduction in Denitrification Nature V. 462 117 2009.
ISSN: ISSN 0028-0836
PubMed: 19890332
DOI: 10.1038/NATURE08507
Page generated: Sun Dec 13 14:59:05 2020

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