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Iron in PDB 3ziy: Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.01 A Resolution

Enzymatic activity of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.01 A Resolution

All present enzymatic activity of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.01 A Resolution:
1.7.2.1;

Protein crystallography data

The structure of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.01 A Resolution, PDB code: 3ziy was solved by S.V.Antonyuk, C.Han, R.R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.76 / 1.01
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 128.177, 128.177, 86.314, 90.00, 90.00, 120.00
R / Rfree (%) 10.9 / 12.2

Other elements in 3ziy:

The structure of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.01 A Resolution also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.01 A Resolution (pdb code 3ziy). 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 Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.01 A Resolution, PDB code: 3ziy:

Iron binding site 1 out of 1 in 3ziy

Go back to Iron Binding Sites List in 3ziy
Iron binding site 1 out of 1 in the Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.01 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.01 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:7.0
occ:1.00
 FE A:HEC600 0.0 7.0 1.0
NC A:HEC600 2.0 6.9 1.0
ND A:HEC600 2.0 7.0 1.0
NB A:HEC600 2.0 7.1 1.0
NA A:HEC600 2.0 7.0 1.0
NE2 A:HIS368 2.0 7.2 1.0
SD A:MET418 2.3 7.6 1.0
CE1 A:HIS368 3.0 7.5 1.0
C4C A:HEC600 3.0 7.4 1.0
C1C A:HEC600 3.0 6.9 1.0
C1D A:HEC600 3.0 7.4 1.0
C1B A:HEC600 3.0 7.3 1.0
C1A A:HEC600 3.0 7.0 1.0
C4B A:HEC600 3.0 7.1 1.0
C4A A:HEC600 3.0 7.5 1.0
C4D A:HEC600 3.0 7.2 1.0
CD2 A:HIS368 3.1 7.1 1.0
HE1 A:HIS368 3.1 7.0 1.0
HD2 A:HIS368 3.3 6.7 1.0
HG3 A:MET418 3.3 7.8 1.0
CHD A:HEC600 3.4 7.7 1.0
CHB A:HEC600 3.4 7.8 1.0
CHC A:HEC600 3.4 6.9 1.0
CE A:MET418 3.4 8.8 1.0
CHA A:HEC600 3.4 7.2 1.0
CG A:MET418 3.4 7.7 1.0
HE1 A:MET418 3.5 8.7 1.0
HE2 A:MET418 3.5 8.6 1.0
HB2 A:MET418 3.7 8.2 1.0
ND1 A:HIS368 4.1 7.8 1.0
CB A:MET418 4.1 8.1 1.0
CG A:HIS368 4.2 7.5 1.0
HG2 A:MET418 4.2 7.8 1.0
C2C A:HEC600 4.2 7.5 1.0
HE3 A:MET418 4.3 9.4 1.0
C3C A:HEC600 4.3 7.6 1.0
C2B A:HEC600 4.3 7.3 1.0
C3A A:HEC600 4.3 7.7 1.0
C2A A:HEC600 4.3 7.5 1.0
C3D A:HEC600 4.3 7.6 1.0
C2D A:HEC600 4.3 7.7 1.0
C3B A:HEC600 4.3 6.9 1.0
HHD A:HEC600 4.5 7.7 1.0
HHC A:HEC600 4.5 6.3 1.0
HHB A:HEC600 4.5 7.5 1.0
HHA A:HEC600 4.5 6.6 1.0
HD22 A:LEU382 4.6 11.3 1.0
HB3 A:MET418 4.6 8.2 1.0
HG23 A:ILE398 4.8 9.3 1.0
HD12 A:LEU382 4.8 9.9 1.0
HG22 A:ILE398 4.8 9.1 1.0
HD1 A:HIS368 4.9 7.8 1.0

Reference:

S.V.Antonyuk, C.Han, R.R.Eady, S.S.Hasnain. Structures of Protein-Protein Complexes Involved in Electron Transfer. Nature V. 496 123 2013.
ISSN: ESSN 1476-4687
PubMed: 23535590
DOI: 10.1038/NATURE11996
Page generated: Sun Aug 4 23:12:56 2024

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