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Copper in PDB 1et5: Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6

Enzymatic activity of Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6

All present enzymatic activity of Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6:
1.7.99.3;

Protein crystallography data

The structure of Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6, PDB code: 1et5 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 / 1.90
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 127.940, 127.940, 66.426, 90.00, 90.00, 120.00
R / Rfree (%) 18.5 / 21.4

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Nitrite Reductase ASP98ASN Mutant From Alcaligenes Faecalis S-6 (pdb code 1et5). 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 ASP98ASN Mutant From Alcaligenes Faecalis S-6, PDB code: 1et5:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1et5

Go back to Copper Binding Sites List in 1et5
Copper binding site 1 out of 2 in the Crystal Structure of Nitrite Reductase ASP98ASN 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 ASP98ASN Mutant From Alcaligenes Faecalis S-6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:27.1
occ:1.00
ND1 A:HIS145 2.0 23.9 1.0
ND1 A:HIS95 2.1 25.0 1.0
SG A:CYS136 2.2 20.2 1.0
SD A:MET150 2.5 23.5 1.0
CE1 A:HIS145 2.9 24.6 1.0
CE1 A:HIS95 3.0 25.8 1.0
CG A:HIS95 3.1 23.9 1.0
CG A:HIS145 3.1 26.2 1.0
CB A:CYS136 3.1 20.5 1.0
CE A:MET150 3.4 19.8 1.0
CB A:HIS95 3.5 24.4 1.0
CB A:HIS145 3.5 19.6 1.0
CA A:HIS95 3.8 23.7 1.0
CG A:MET150 4.0 22.3 1.0
NE2 A:HIS145 4.1 25.1 1.0
NE2 A:HIS95 4.1 27.6 1.0
CD2 A:HIS145 4.2 24.7 1.0
O A:MET94 4.2 24.3 1.0
CD2 A:HIS95 4.2 24.9 1.0
CG A:PRO138 4.2 28.4 1.0
SD A:MET62 4.4 27.6 1.0
CB A:MET150 4.4 21.6 1.0
CA A:CYS136 4.5 20.0 1.0
N A:ASN96 4.7 22.6 1.0
CD A:PRO138 4.8 26.3 1.0
CA A:HIS145 4.8 20.4 1.0
CB A:MET62 4.8 26.4 1.0
C A:HIS95 4.8 24.8 1.0
N A:HIS95 4.9 25.7 1.0
C A:MET94 5.0 24.9 1.0

Copper binding site 2 out of 2 in 1et5

Go back to Copper Binding Sites List in 1et5
Copper binding site 2 out of 2 in the Crystal Structure of Nitrite Reductase ASP98ASN 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 ASP98ASN Mutant From Alcaligenes Faecalis S-6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:22.6
occ:1.00
NE2 A:HIS100 2.0 15.9 1.0
NE2 A:HIS135 2.1 20.8 1.0
O A:HOH503 2.2 15.3 1.0
CE1 A:HIS100 2.8 15.1 1.0
CE1 A:HIS135 3.1 18.9 1.0
CD2 A:HIS100 3.1 17.2 1.0
CD2 A:HIS135 3.1 20.5 1.0
ND1 A:HIS100 4.0 15.5 1.0
CG A:HIS100 4.2 14.6 1.0
ND1 A:HIS135 4.2 17.1 1.0
CG A:HIS135 4.3 19.6 1.0
O A:HOH582 4.3 38.7 1.0
ND2 A:ASN98 4.4 26.7 1.0
CG A:ASN98 4.7 27.7 1.0
OD1 A:ASN98 4.7 25.6 1.0
O A:HOH1098 5.0 24.4 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 21:42:00 2020
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