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Iron in PDB 2zoo: Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125

Enzymatic activity of Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125

All present enzymatic activity of Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125:
1.7.2.1; 1.7.99.3;

Protein crystallography data

The structure of Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125, PDB code: 2zoo was solved by M.Nojiri, A.Tsuda, 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 / 1.95
Space group P 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 180.338, 180.338, 180.338, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 18.6

Other elements in 2zoo:

The structure of Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125 also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125 (pdb code 2zoo). 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 Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125, PDB code: 2zoo:

Iron binding site 1 out of 1 in 2zoo

Go back to Iron Binding Sites List in 2zoo
Iron binding site 1 out of 1 in the Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125


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 Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:20.4
occ:1.00
FE A:HEM600 0.0 20.4 1.0
NE2 A:HIS354 2.0 19.9 1.0
NB A:HEM600 2.1 16.4 1.0
NA A:HEM600 2.1 21.3 1.0
ND A:HEM600 2.1 19.2 1.0
NC A:HEM600 2.1 19.1 1.0
SD A:MET404 2.4 20.5 1.0
CE1 A:HIS354 3.0 18.9 1.0
CD2 A:HIS354 3.0 18.1 1.0
C4B A:HEM600 3.0 20.9 1.0
C1A A:HEM600 3.0 20.7 1.0
C4D A:HEM600 3.1 19.4 1.0
C1C A:HEM600 3.1 17.8 1.0
C1B A:HEM600 3.1 20.8 1.0
C4A A:HEM600 3.1 21.2 1.0
C4C A:HEM600 3.1 19.4 1.0
C1D A:HEM600 3.1 19.7 1.0
CHA A:HEM600 3.3 19.2 1.0
CHC A:HEM600 3.3 18.8 1.0
CHB A:HEM600 3.4 19.9 1.0
CHD A:HEM600 3.4 18.6 1.0
CG A:MET404 3.5 19.2 1.0
CE A:MET404 3.5 18.9 1.0
ND1 A:HIS354 4.1 19.3 1.0
CB A:MET404 4.1 21.0 1.0
CG A:HIS354 4.1 19.0 1.0
C2B A:HEM600 4.2 21.1 1.0
C3B A:HEM600 4.2 19.2 1.0
C2A A:HEM600 4.3 21.9 1.0
C3A A:HEM600 4.3 21.5 1.0
C2C A:HEM600 4.3 18.0 1.0
C2D A:HEM600 4.3 18.1 1.0
C3D A:HEM600 4.3 19.6 1.0
C3C A:HEM600 4.3 18.6 1.0

Reference:

M.Nojiri, H.Koteishi, A.Tsuda, T.Nakagami, K.Kobayashi, T.Inoue, K.Yamaguchi, S.Suzuki. Electron Transfer Processes Within and Between Proteins Containing the Heme C and Blue Cu To Be Published.
Page generated: Sun Dec 13 14:59:05 2020

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