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Iron in PDB 6f1q: Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group

Enzymatic activity of Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group

All present enzymatic activity of Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group:
1.7.2.1;

Protein crystallography data

The structure of Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group, PDB code: 6f1q was solved by S.Antonyuk, D.Sasaki, 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) 50.00 / 2.30
Space group I 21 3
Cell size a, b, c (Å), α, β, γ (°) 180.853, 180.853, 180.853, 90.00, 90.00, 90.00
R / Rfree (%) 13.4 / 16.2

Other elements in 6f1q:

The structure of Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group (pdb code 6f1q). 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 Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group, PDB code: 6f1q:

Iron binding site 1 out of 1 in 6f1q

Go back to Iron Binding Sites List in 6f1q
Iron binding site 1 out of 1 in the Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group


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 Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe503

b:44.1
occ:1.00
 FE A:HEC503 0.0 44.1 1.0
ND A:HEC503 1.9 52.5 1.0
NE2 A:HIS368 2.0 42.0 1.0
NA A:HEC503 2.0 53.6 1.0
NC A:HEC503 2.1 45.8 1.0
NB A:HEC503 2.1 49.5 1.0
SD A:MET418 2.2 42.9 1.0
CE1 A:HIS368 2.9 47.6 1.0
C1D A:HEC503 2.9 48.9 1.0
C4D A:HEC503 2.9 48.3 1.0
C4A A:HEC503 3.0 53.9 1.0
C1A A:HEC503 3.0 51.1 1.0
C4B A:HEC503 3.0 47.1 1.0
C1B A:HEC503 3.0 51.4 1.0
CD2 A:HIS368 3.0 47.4 1.0
C4C A:HEC503 3.1 44.6 1.0
C1C A:HEC503 3.1 43.4 1.0
CG A:MET418 3.3 48.7 1.0
CE A:MET418 3.4 50.2 1.0
CHA A:HEC503 3.4 47.2 1.0
CHD A:HEC503 3.4 46.1 1.0
CHB A:HEC503 3.4 48.5 1.0
CHC A:HEC503 3.4 42.5 1.0
ND1 A:HIS368 4.0 45.4 1.0
CG A:HIS368 4.1 41.1 1.0
CB A:MET418 4.2 47.5 1.0
C2D A:HEC503 4.2 46.1 1.0
C3D A:HEC503 4.2 49.5 1.0
C3A A:HEC503 4.2 55.1 1.0
C2A A:HEC503 4.2 53.7 1.0
C3C A:HEC503 4.3 42.7 1.0
C2C A:HEC503 4.3 47.3 1.0
C2B A:HEC503 4.3 47.9 1.0
C3B A:HEC503 4.3 46.2 1.0

Reference:

J.Dong, D.Sasaki, R.Eady, S.V.Antonyuk, S.S.Hasnain. Substrate Entry and Binding Requires Activation of Tyrosine in Heme-Copper Nitrite Reductase To Be Published.
Page generated: Tue Aug 6 17:59:19 2024

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