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Copper in PDB 4csz: Structure of F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans with Nitrite Bound

Enzymatic activity of Structure of F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans with Nitrite Bound

All present enzymatic activity of Structure of F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans with Nitrite Bound:
1.7.2.1;

Protein crystallography data

The structure of Structure of F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans with Nitrite Bound, PDB code: 4csz was solved by N.G.H.Leferink, S.V.Antonyuk, J.A.Houwman, N.S.Scrutton, R.Ready, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.29 / 1.75
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 89.570, 89.570, 144.011, 90.00, 90.00, 120.00
R / Rfree (%) 17.821 / 20.993

Other elements in 4csz:

The structure of Structure of F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans with Nitrite Bound also contains other interesting chemical elements:

Zinc (Zn) 7 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Structure of F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans with Nitrite Bound (pdb code 4csz). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structure of F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans with Nitrite Bound, PDB code: 4csz:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 4csz

Go back to Copper Binding Sites List in 4csz
Copper binding site 1 out of 2 in the Structure of F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans with Nitrite Bound


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans with Nitrite Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1337

b:25.9
occ:1.00
ND1 A:HIS139 2.0 23.8 1.0
SG A:CYS130 2.1 26.2 1.0
ND1 A:HIS89 2.2 26.5 1.0
SD A:MET144 2.7 24.1 0.8
CE1 A:HIS139 2.9 25.0 1.0
CB A:CYS130 3.0 23.5 1.0
CG A:HIS139 3.1 23.7 1.0
CE1 A:HIS89 3.1 29.2 1.0
CG A:HIS89 3.2 29.0 1.0
CB A:HIS89 3.5 28.3 1.0
CB A:HIS139 3.5 21.6 1.0
CE A:MET144 3.5 22.3 0.8
CA A:HIS89 3.8 29.1 1.0
CG A:PRO132 3.9 29.0 1.0
NE2 A:HIS139 4.0 27.0 1.0
O A:PRO88 4.1 27.1 1.0
CD2 A:HIS139 4.2 24.4 1.0
CG A:MET144 4.2 22.6 1.0
NE2 A:HIS89 4.3 28.1 1.0
CD A:PRO132 4.3 27.1 1.0
CD2 A:HIS89 4.3 28.4 1.0
CA A:CYS130 4.5 22.0 1.0
SD A:MET56 4.6 26.8 1.0
CB A:MET144 4.6 21.4 1.0
CA A:HIS139 4.7 19.2 1.0
N A:ASN90 4.7 28.7 1.0
N A:HIS89 4.8 29.6 1.0
C A:PRO88 4.9 31.2 1.0
C A:HIS89 4.9 31.4 1.0
C A:CYS130 4.9 25.1 1.0

Copper binding site 2 out of 2 in 4csz

Go back to Copper Binding Sites List in 4csz
Copper binding site 2 out of 2 in the Structure of F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans with Nitrite Bound


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans with Nitrite Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1338

b:20.7
occ:1.00
O1 A:NO21340 1.9 36.2 1.0
N A:NO21340 2.0 43.4 1.0
NE2 A:HIS129 2.0 20.1 1.0
NE2 A:HIS94 2.1 21.3 1.0
O2 A:NO21340 2.4 43.3 1.0
CE1 A:HIS94 2.9 19.8 1.0
CD2 A:HIS129 3.0 18.8 1.0
CE1 A:HIS129 3.0 19.9 1.0
CD2 A:HIS94 3.2 19.8 1.0
OD2 A:ASP92 3.6 30.1 1.0
ND1 A:HIS94 4.1 20.2 1.0
ND1 A:HIS129 4.1 19.2 1.0
CG A:HIS129 4.2 20.1 1.0
CG A:HIS94 4.2 19.5 1.0
CG A:ASP92 4.3 26.7 1.0
OD1 A:ASP92 4.7 23.1 1.0
O A:HOH2116 4.9 31.2 1.0

Reference:

N.G.H.Leferink, S.V.Antonyuk, J.A.Houwman, N.S.Scrutton, R.R.Eady, S.S.Hasnain. Impact of Residues Remote From the Catalytic Centre on Enzyme Catalysis of Copper Nitrite Reductase. Nat.Commun. V. 5 4395 2014.
ISSN: ISSN 2041-1723
PubMed: 25022223
DOI: 10.1038/NCOMMS5395
Page generated: Sun Dec 13 11:13:49 2020

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