Copper in PDB 6fja: Crystal Structure of T2D Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii

Enzymatic activity of Crystal Structure of T2D Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii

All present enzymatic activity of Crystal Structure of T2D Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii:
1.7.2.1;

Protein crystallography data

The structure of Crystal Structure of T2D Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 6fja was solved by S.V.Antonyuk, R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.66 / 2.20
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 128.230, 128.230, 86.110, 90.00, 90.00, 120.00
R / Rfree (%) 13.6 / 17.5

Other elements in 6fja:

The structure of Crystal Structure of T2D Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii also contains other interesting chemical elements:

Iron (Fe) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of T2D Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii (pdb code 6fja). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of T2D Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 6fja:

Copper binding site 1 out of 1 in 6fja

Go back to Copper Binding Sites List in 6fja
Copper binding site 1 out of 1 in the Crystal Structure of T2D Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of T2D Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:25.2
occ:1.00
 ND1 A:HIS94 2.1 21.1 1.0
SG A:CYS135 2.2 22.8 1.0
ND1 A:HIS143 2.2 22.1 1.0
SD A:MET148 2.6 25.1 1.0
CE1 A:HIS94 3.1 22.2 1.0
CE1 A:HIS143 3.1 22.8 1.0
CB A:CYS135 3.1 22.2 1.0
CG A:HIS143 3.1 21.4 1.0
CG A:HIS94 3.2 20.9 1.0
CB A:HIS143 3.5 21.2 1.0
CE A:MET148 3.5 23.8 1.0
CB A:HIS94 3.5 20.6 1.0
CA A:HIS94 3.8 20.7 1.0
O A:PRO93 4.1 19.4 1.0
CG A:MET148 4.1 23.5 1.0
NE2 A:HIS143 4.2 22.7 1.0
NE2 A:HIS94 4.2 22.3 1.0
CD2 A:HIS143 4.2 21.9 1.0
OG1 A:THR137 4.3 25.1 1.0
CD2 A:HIS94 4.3 21.3 1.0
CB A:THR137 4.4 24.6 1.0
CE3 A:TRP61 4.6 22.6 1.0
CA A:CYS135 4.6 22.0 1.0
N A:ASN95 4.6 20.1 1.0
CB A:MET148 4.6 22.3 1.0
CA A:HIS143 4.6 22.1 1.0
C A:HIS94 4.8 20.1 1.0
N A:HIS94 4.8 21.6 1.0
C A:PRO93 4.8 22.1 1.0

Reference:

J.Dong, D.Sasaki, R.Eady, S.V.Antonyuk, S.S.Hasnain. Activation of Redox Tyrosine Switch Is Required For Ligand Binding at the Catalytic Site in Heme-Cu Nitrite Reductases To Be Published.
Page generated: Wed Jul 31 06:05:42 2024

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