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Copper in PDB 3h56: MET150LEU/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis

Enzymatic activity of MET150LEU/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis

All present enzymatic activity of MET150LEU/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis:
1.7.2.1;

Protein crystallography data

The structure of MET150LEU/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis, PDB code: 3h56 was solved by I.S.Macpherson, F.I.Rosell, M.Scofield, A.G.Mauk, M.E.P.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.50
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 126.724, 126.724, 65.062, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 20.4

Copper Binding Sites:

The binding sites of Copper atom in the MET150LEU/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis (pdb code 3h56). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the MET150LEU/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis, PDB code: 3h56:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3h56

Go back to Copper Binding Sites List in 3h56
Copper binding site 1 out of 2 in the MET150LEU/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of MET150LEU/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu340

b:19.9
occ:1.00
ND1 A:HIS145 2.0 17.0 1.0
SG A:CYS136 2.1 17.3 1.0
ND1 A:HIS95 2.1 20.1 1.0
CE1 A:HIS145 2.9 23.9 1.0
CG A:HIS145 3.0 19.6 1.0
CD2 A:LEU150 3.0 17.9 1.0
CE1 A:HIS95 3.1 20.0 1.0
CG A:HIS95 3.1 19.6 1.0
CB A:CYS136 3.3 18.5 1.0
CB A:HIS95 3.4 20.5 1.0
CB A:HIS145 3.4 19.4 1.0
CA A:HIS95 3.6 20.1 1.0
CG A:PRO138 3.7 23.0 1.0
O A:MET94 3.8 21.3 1.0
NE2 A:HIS145 4.0 21.0 1.0
CD2 A:HIS145 4.1 21.2 1.0
NE2 A:HIS95 4.2 19.2 1.0
CD A:PRO138 4.2 22.8 1.0
CD2 A:HIS95 4.2 21.4 1.0
CG A:LEU150 4.4 21.4 1.0
SD A:MET62 4.5 21.6 1.0
N A:HIS95 4.5 20.4 1.0
N A:ASN96 4.6 20.0 1.0
C A:MET94 4.6 20.7 1.0
C A:HIS95 4.7 20.0 1.0
CA A:CYS136 4.7 18.3 1.0
CA A:HIS145 4.8 19.0 1.0
CB A:LEU150 4.9 19.1 1.0
CB A:PRO138 5.0 22.4 1.0

Copper binding site 2 out of 2 in 3h56

Go back to Copper Binding Sites List in 3h56
Copper binding site 2 out of 2 in the MET150LEU/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of MET150LEU/PHE312CYS Variant of Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu341

b:19.4
occ:1.00
NE2 A:HIS100 1.9 12.6 1.0
NE2 A:HIS135 2.1 16.2 1.0
CE1 A:HIS100 2.8 16.8 1.0
CD2 A:HIS135 3.0 14.8 1.0
CD2 A:HIS100 3.1 17.6 1.0
CE1 A:HIS135 3.1 18.5 1.0
OD1 A:ASP98 3.4 26.8 1.0
ND1 A:HIS100 4.0 16.4 1.0
CG A:HIS100 4.1 15.8 1.0
CG A:ASP98 4.1 21.4 1.0
CG A:HIS135 4.2 17.2 1.0
ND1 A:HIS135 4.2 16.3 1.0
OD2 A:ASP98 4.5 20.0 1.0

Reference:

I.S.Macpherson, F.I.Rosell, M.Scofield, A.G.Mauk, M.E.Murphy. Directed Evolution of Copper Nitrite Reductase to A Chromogenic Reductant. Protein Eng.Des.Sel. V. 23 137 2010.
ISSN: ISSN 1741-0126
PubMed: 20083495
DOI: 10.1093/PROTEIN/GZP084
Page generated: Thu Sep 3 17:17:23 2020
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