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Copper in PDB 1tho: Crystal Structure of A Mutant Escherichia Coli Thioredoxin with An Arginine Insertion in the Active Site

Protein crystallography data

The structure of Crystal Structure of A Mutant Escherichia Coli Thioredoxin with An Arginine Insertion in the Active Site, PDB code: 1tho was solved by M.Nikkola, K.Langsetmo, J.A.Fuchs, H.Eklund, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.30
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 78.400, 78.400, 35.100, 90.00, 90.00, 120.00
R / Rfree (%) 17.3 / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of A Mutant Escherichia Coli Thioredoxin with An Arginine Insertion in the Active Site (pdb code 1tho). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of A Mutant Escherichia Coli Thioredoxin with An Arginine Insertion in the Active Site, PDB code: 1tho:

Copper binding site 1 out of 1 in 1tho

Go back to Copper Binding Sites List in 1tho
Copper binding site 1 out of 1 in the Crystal Structure of A Mutant Escherichia Coli Thioredoxin with An Arginine Insertion in the Active Site


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 A Mutant Escherichia Coli Thioredoxin with An Arginine Insertion in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu109

b:44.2
occ:1.00
OD1 A:ASP2 1.8 78.5 1.0
N A:ASP2 2.1 78.4 1.0
N A:SER1 2.6 84.9 1.0
CG A:ASP2 2.7 80.4 1.0
C A:SER1 3.0 81.6 1.0
CB A:ASP2 3.1 79.7 1.0
CA A:ASP2 3.1 75.4 1.0
CA A:SER1 3.2 83.4 1.0
OD2 A:ASP2 3.9 80.8 1.0
N A:LYS3 4.1 59.5 1.0
O A:SER1 4.1 83.7 1.0
C A:ASP2 4.2 69.5 1.0
OD1 A:ASP43 4.4 24.7 1.0
CB A:SER1 4.5 85.0 1.0
CG A:ASP43 4.8 29.6 1.0

Reference:

M.Nikkola, K.Langsetmo, J.A.Fuchs, H.Eklund. Crystal Structure of A Mutant Escherichia Coli Thioredoxin with An Arginine Insertion in the Active Site To Be Published.
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