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Iron in PDB 3zbm: Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii

Enzymatic activity of Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii

All present enzymatic activity of Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii:
1.7.2.1;

Protein crystallography data

The structure of Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 3zbm 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) 40.14 / 1.87
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 128.410, 128.410, 86.090, 90.00, 90.00, 120.00
R / Rfree (%) 13.9 / 16.8

Other elements in 3zbm:

The structure of Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii (pdb code 3zbm). 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 M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 3zbm:

Iron binding site 1 out of 1 in 3zbm

Go back to Iron Binding Sites List in 3zbm
Iron binding site 1 out of 1 in the Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1462

b:18.7
occ:1.00
 FE A:HEC1462 0.0 18.7 1.0
NB A:HEC1462 2.0 19.4 1.0
NE2 A:HIS368 2.0 16.7 1.0
NC A:HEC1462 2.0 18.7 1.0
NA A:HEC1462 2.0 16.6 1.0
ND A:HEC1462 2.0 17.4 1.0
SD A:MET418 2.3 20.0 1.0
CE1 A:HIS368 2.9 18.4 1.0
C4C A:HEC1462 3.0 19.3 1.0
C1B A:HEC1462 3.0 15.9 1.0
C1D A:HEC1462 3.0 18.1 1.0
C4B A:HEC1462 3.0 18.9 1.0
CD2 A:HIS368 3.1 18.6 1.0
C1A A:HEC1462 3.1 19.0 1.0
C1C A:HEC1462 3.1 19.8 1.0
C4A A:HEC1462 3.1 19.8 1.0
C4D A:HEC1462 3.1 18.1 1.0
CHD A:HEC1462 3.3 16.7 1.0
CE A:MET418 3.4 18.6 1.0
CHB A:HEC1462 3.4 18.6 1.0
CG A:MET418 3.4 19.6 1.0
CHC A:HEC1462 3.4 18.2 1.0
CHA A:HEC1462 3.5 18.6 1.0
ND1 A:HIS368 4.1 19.1 1.0
CB A:MET418 4.1 21.1 1.0
CG A:HIS368 4.2 19.6 1.0
C3C A:HEC1462 4.2 19.9 1.0
C3B A:HEC1462 4.2 18.4 1.0
C2B A:HEC1462 4.2 16.0 1.0
C2C A:HEC1462 4.3 20.2 1.0
C2A A:HEC1462 4.3 19.0 1.0
C3A A:HEC1462 4.3 19.2 1.0
C2D A:HEC1462 4.3 18.3 1.0
C3D A:HEC1462 4.3 18.9 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 Dec 13 15:26:42 2020

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