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Copper in PDB 1et8: Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis

Enzymatic activity of Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis

All present enzymatic activity of Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis:
1.7.99.3;

Protein crystallography data

The structure of Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis, PDB code: 1et8 was solved by M.J.Boulanger, M.Kukimoto, M.Nishiyama, S.Horinouchi, M.E.P.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 500.00 / 1.80
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 127.659, 127.659, 67.215, 90.00, 90.00, 120.00
R / Rfree (%) 18.2 / 21.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis (pdb code 1et8). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis, PDB code: 1et8:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1et8

Go back to Copper Binding Sites List in 1et8
Copper binding site 1 out of 2 in the Crystal Structure of Nitrite Reductase HIS255ASN Mutant 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 Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:28.3
occ:1.00
ND1 A:HIS145 1.9 21.7 1.0
ND1 A:HIS95 2.1 25.9 1.0
SG A:CYS136 2.2 24.6 1.0
SD A:MET150 2.6 25.1 1.0
CE1 A:HIS145 2.8 23.8 1.0
CG A:HIS145 3.1 22.6 1.0
CE1 A:HIS95 3.1 26.9 1.0
CG A:HIS95 3.1 26.0 1.0
CB A:CYS136 3.2 22.5 1.0
CE A:MET150 3.3 22.0 1.0
CB A:HIS95 3.5 25.5 1.0
CB A:HIS145 3.5 22.0 1.0
CA A:HIS95 3.8 26.2 1.0
NE2 A:HIS145 3.9 23.5 1.0
CG A:MET150 4.0 24.2 1.0
CD2 A:HIS145 4.1 23.1 1.0
CG A:PRO138 4.1 27.4 1.0
O A:MET94 4.2 26.8 1.0
NE2 A:HIS95 4.2 25.2 1.0
CD2 A:HIS95 4.2 26.3 1.0
SD A:MET62 4.3 29.9 1.0
CB A:MET150 4.5 22.9 1.0
CA A:CYS136 4.6 22.5 1.0
N A:ASN96 4.6 24.5 1.0
CD A:PRO138 4.7 26.7 1.0
CA A:HIS145 4.8 22.4 1.0
C A:HIS95 4.8 25.0 1.0
N A:HIS95 4.8 26.3 1.0
CB A:MET62 4.9 28.2 1.0
C A:MET94 4.9 27.5 1.0

Copper binding site 2 out of 2 in 1et8

Go back to Copper Binding Sites List in 1et8
Copper binding site 2 out of 2 in the Crystal Structure of Nitrite Reductase HIS255ASN Mutant 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 Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:23.4
occ:1.00
O A:HOH503 1.8 23.8 1.0
NE2 A:HIS100 2.0 20.4 1.0
NE2 A:HIS135 2.1 23.8 1.0
CE1 A:HIS100 2.9 20.7 1.0
CD2 A:HIS100 3.0 19.8 1.0
CD2 A:HIS135 3.1 21.1 1.0
CE1 A:HIS135 3.2 22.2 1.0
O A:HOH1099 3.2 42.3 1.0
OD1 A:ASP98 3.6 26.1 1.0
ND1 A:HIS100 4.0 20.5 1.0
CG A:HIS100 4.1 19.5 1.0
CG A:HIS135 4.2 21.4 1.0
O A:HOH979 4.2 48.9 1.0
ND1 A:HIS135 4.2 20.9 1.0
CG A:ASP98 4.4 25.8 1.0
OD2 A:ASP98 4.7 25.4 1.0
O A:HOH1098 5.0 24.2 1.0

Reference:

M.J.Boulanger, M.Kukimoto, M.Nishiyama, S.Horinouchi, M.E.Murphy. Catalytic Roles For Two Water Bridged Residues (Asp-98 and His-255) in the Active Site of Copper-Containing Nitrite Reductase. J.Biol.Chem. V. 275 23957 2000.
ISSN: ISSN 0021-9258
PubMed: 10811642
DOI: 10.1074/JBC.M001859200
Page generated: Wed Sep 2 21:42:09 2020
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