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Copper in PDB 1et7: Crystal Structure of Nitrite Reductase HIS255ASP Mutant From Alcaligenes Faecalis S-6

Enzymatic activity of Crystal Structure of Nitrite Reductase HIS255ASP Mutant From Alcaligenes Faecalis S-6

All present enzymatic activity of Crystal Structure of Nitrite Reductase HIS255ASP Mutant From Alcaligenes Faecalis S-6:
1.7.99.3;

Protein crystallography data

The structure of Crystal Structure of Nitrite Reductase HIS255ASP Mutant From Alcaligenes Faecalis S-6, PDB code: 1et7 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 / 1.70
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 127.640, 127.640, 67.510, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / 21

Other elements in 1et7:

The structure of Crystal Structure of Nitrite Reductase HIS255ASP Mutant From Alcaligenes Faecalis S-6 also contains other interesting chemical elements:

Cadmium (Cd) 3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Nitrite Reductase HIS255ASP Mutant From Alcaligenes Faecalis S-6 (pdb code 1et7). 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 HIS255ASP Mutant From Alcaligenes Faecalis S-6, PDB code: 1et7:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1et7

Go back to Copper Binding Sites List in 1et7
Copper binding site 1 out of 2 in the Crystal Structure of Nitrite Reductase HIS255ASP Mutant From Alcaligenes Faecalis S-6


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 HIS255ASP Mutant From Alcaligenes Faecalis S-6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:23.8
occ:1.00
ND1 A:HIS145 2.0 18.7 1.0
ND1 A:HIS95 2.1 22.3 1.0
SG A:CYS136 2.2 21.5 1.0
SD A:MET150 2.5 21.7 1.0
CE1 A:HIS145 2.8 20.9 1.0
CE1 A:HIS95 3.0 22.3 1.0
CG A:HIS145 3.1 21.8 1.0
CG A:HIS95 3.1 22.7 1.0
CB A:CYS136 3.2 19.8 1.0
CE A:MET150 3.2 22.3 1.0
CB A:HIS95 3.5 22.3 1.0
CB A:HIS145 3.5 20.7 1.0
CA A:HIS95 3.9 23.1 1.0
NE2 A:HIS145 4.0 20.4 1.0
CG A:MET150 4.0 22.7 1.0
CD2 A:HIS145 4.1 20.9 1.0
NE2 A:HIS95 4.1 21.6 1.0
CG A:PRO138 4.2 24.2 1.0
CD2 A:HIS95 4.2 23.3 1.0
O A:MET94 4.3 23.1 1.0
SD A:MET62 4.3 24.3 1.0
CB A:MET150 4.4 20.3 1.0
CA A:CYS136 4.6 19.2 1.0
N A:ASN96 4.7 21.4 1.0
CD A:PRO138 4.7 22.1 1.0
CA A:HIS145 4.8 21.0 1.0
CB A:MET62 4.8 24.3 1.0
C A:HIS95 4.9 22.4 1.0
N A:HIS95 4.9 21.4 1.0

Copper binding site 2 out of 2 in 1et7

Go back to Copper Binding Sites List in 1et7
Copper binding site 2 out of 2 in the Crystal Structure of Nitrite Reductase HIS255ASP Mutant From Alcaligenes Faecalis S-6


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 HIS255ASP Mutant From Alcaligenes Faecalis S-6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:18.5
occ:1.00
O A:HOH503 1.8 36.4 1.0
NE2 A:HIS100 2.1 19.2 1.0
NE2 A:HIS135 2.2 20.2 1.0
O A:HOH1099 2.5 29.6 1.0
CE1 A:HIS100 3.0 17.6 1.0
CD2 A:HIS100 3.2 17.6 1.0
OD1 A:ASP98 3.2 26.1 1.0
CD2 A:HIS135 3.2 18.9 1.0
CE1 A:HIS135 3.2 18.1 1.0
O A:HOH822 3.7 37.2 1.0
CG A:ASP98 4.1 26.6 1.0
ND1 A:HIS100 4.2 18.5 1.0
CG A:HIS100 4.3 18.6 1.0
ND1 A:HIS135 4.3 17.8 1.0
CG A:HIS135 4.3 19.5 1.0
OD2 A:ASP98 4.6 25.5 1.0
O A:HOH1098 4.7 22.9 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: Sun Dec 13 10:58:41 2020

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