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Copper in PDB 4hu9: E. Coli Thioredoxin Variant with (4S)-FLUOROPRO76 As Single Proline Residue

Protein crystallography data

The structure of E. Coli Thioredoxin Variant with (4S)-FLUOROPRO76 As Single Proline Residue, PDB code: 4hu9 was solved by M.A.Scharer, M.Rubini, G.Capitani, R.Glockshuber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.18 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.270, 48.760, 31.570, 90.00, 101.94, 90.00
R / Rfree (%) 17.3 / 21

Other elements in 4hu9:

The structure of E. Coli Thioredoxin Variant with (4S)-FLUOROPRO76 As Single Proline Residue also contains other interesting chemical elements:

Fluorine (F) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the E. Coli Thioredoxin Variant with (4S)-FLUOROPRO76 As Single Proline Residue (pdb code 4hu9). 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 E. Coli Thioredoxin Variant with (4S)-FLUOROPRO76 As Single Proline Residue, PDB code: 4hu9:

Copper binding site 1 out of 1 in 4hu9

Go back to Copper Binding Sites List in 4hu9
Copper binding site 1 out of 1 in the E. Coli Thioredoxin Variant with (4S)-FLUOROPRO76 As Single Proline Residue


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of E. Coli Thioredoxin Variant with (4S)-FLUOROPRO76 As Single Proline Residue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:14.9
occ:0.93
N A:ASP2 1.9 13.5 1.0
N A:SER1 2.0 15.1 0.6
N A:SER1 2.0 14.4 0.4
OD1 A:ASP2 2.0 12.0 1.0
C A:SER1 2.7 15.2 0.6
C A:SER1 2.7 14.1 0.4
CA A:SER1 2.8 16.6 0.6
CA A:SER1 2.8 14.2 0.4
CG A:ASP2 2.9 11.0 1.0
CA A:ASP2 3.0 12.2 1.0
CB A:ASP2 3.2 12.4 1.0
O A:HOH365 3.5 21.8 1.0
N A:LYS3 3.6 7.8 1.0
C A:ASP2 3.8 8.8 1.0
O A:SER1 3.9 16.0 0.6
O A:SER1 3.9 14.6 0.4
OD2 A:ASP2 4.1 10.2 1.0
CB A:SER1 4.1 20.0 0.6
CB A:SER1 4.1 14.4 0.4
OD1 A:ASP43 4.1 10.2 1.0
OG A:SER1 4.2 22.2 0.6
CG A:ASP43 4.5 8.2 1.0
OD2 A:ASP43 4.7 8.7 1.0
CG A:LYS3 4.9 8.0 1.0
CA A:LYS3 4.9 7.4 1.0
OG A:SER1 5.0 13.5 0.4

Reference:

M.Rubini, M.A.Scharer, G.Capitani, R.Glockshuber. (4R)- and (4S)-Fluoroproline in the Conserved Cis-Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering. Chembiochem V. 14 1053 2013.
ISSN: ISSN 1439-4227
PubMed: 23712956
DOI: 10.1002/CBIC.201300178
Page generated: Sun Dec 13 11:14:46 2020

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