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Iron in PDB 2yqb: Structure of P93A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.4 A Resolution

Enzymatic activity of Structure of P93A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.4 A Resolution

All present enzymatic activity of Structure of P93A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.4 A Resolution:
1.7.2.1;

Protein crystallography data

The structure of Structure of P93A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.4 A Resolution, PDB code: 2yqb 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) 18.07 / 1.41
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 127.849, 127.849, 86.628, 90.00, 90.00, 120.00
R / Rfree (%) 11.2 / 14.7

Other elements in 2yqb:

The structure of Structure of P93A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.4 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 P93A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.4 A Resolution (pdb code 2yqb). 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 P93A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.4 A Resolution, PDB code: 2yqb:

Iron binding site 1 out of 1 in 2yqb

Go back to Iron Binding Sites List in 2yqb
Iron binding site 1 out of 1 in the Structure of P93A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.4 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 P93A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii at 1.4 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:7.4
occ:1.00
 FE A:HEC600 0.0 7.4 1.0
NC A:HEC600 2.0 6.1 1.0
NA A:HEC600 2.0 6.2 1.0
ND A:HEC600 2.0 6.6 1.0
NE2 A:HIS368 2.0 6.1 1.0
NB A:HEC600 2.1 7.0 1.0
SD A:MET418 2.3 7.6 1.0
CE1 A:HIS368 3.0 7.0 1.0
C1D A:HEC600 3.0 6.3 1.0
C4C A:HEC600 3.0 7.0 1.0
C4A A:HEC600 3.0 6.3 1.0
C1A A:HEC600 3.0 8.2 1.0
C1C A:HEC600 3.0 6.3 1.0
CD2 A:HIS368 3.1 6.3 1.0
C4D A:HEC600 3.1 7.1 1.0
C1B A:HEC600 3.1 6.6 1.0
C4B A:HEC600 3.1 6.2 1.0
CHD A:HEC600 3.4 6.6 1.0
CHB A:HEC600 3.4 6.4 1.0
CE A:MET418 3.4 9.3 1.0
CHA A:HEC600 3.4 6.3 1.0
CHC A:HEC600 3.4 7.2 1.0
CG A:MET418 3.4 8.4 1.0
ND1 A:HIS368 4.1 6.7 1.0
CG A:HIS368 4.2 6.2 1.0
CB A:MET418 4.2 8.1 1.0
C2A A:HEC600 4.2 7.0 1.0
C3A A:HEC600 4.3 7.5 1.0
C2C A:HEC600 4.3 6.5 1.0
C3C A:HEC600 4.3 6.4 1.0
C3B A:HEC600 4.3 7.3 1.0
C2D A:HEC600 4.3 7.1 1.0
C2B A:HEC600 4.3 5.2 1.0
C3D A:HEC600 4.3 8.5 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: Thu Jul 17 06:15:21 2025

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