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

The structure of E. Coli Thioredoxin Variant with (4R)-FLUOROPRO76 As Single Proline Residue, PDB code: 4hua 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)	43.22 / 1.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	88.360, 48.690, 31.490, 90.00, 101.98, 90.00
R / Rfree (%)	15.9 / 17.2

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

Fluorine

(F)

1 atom

The binding sites of Copper atom in the E. Coli Thioredoxin Variant with (4R)-FLUOROPRO76 As Single Proline Residue (pdb code 4hua). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the E. Coli Thioredoxin Variant with (4R)-FLUOROPRO76 As Single Proline Residue, PDB code: 4hua:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the E. Coli Thioredoxin Variant with (4R)-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 (4R)-FLUOROPRO76 As Single Proline Residue within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:13.4 occ:0.30 CU A:CU201 0.0 13.4 0.3 CU A:CU201 1.1 7.3 0.5 N A:SER1 1.9 13.8 1.0 N A:ASP2 2.0 11.9 1.0 O A:HOH351 2.3 29.1 1.0 OD1 A:ASP2 2.6 13.0 1.0 CA A:SER1 2.7 15.0 1.0 C A:SER1 2.7 13.8 1.0 OG A:SER1 3.1 22.6 1.0 CA A:ASP2 3.1 11.8 1.0 CB A:ASP2 3.3 12.2 1.0 CG A:ASP2 3.3 12.2 1.0 CB A:SER1 3.5 19.5 1.0 O A:HOH314 3.6 15.7 1.0 O A:SER1 4.0 15.4 1.0 C A:ASP2 4.2 11.7 1.0 N A:LYS3 4.2 11.3 1.0 OD1 A:ASP43 4.5 14.0 1.0 OD2 A:ASP2 4.5 11.8 1.0 CG A:ASP43 4.9 12.5 1.0 OD2 A:ASP43 4.9 13.0 1.0

Copper binding site 2 out of 2 in the E. Coli Thioredoxin Variant with (4R)-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 2 of E. Coli Thioredoxin Variant with (4R)-FLUOROPRO76 As Single Proline Residue within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:7.3 occ:0.50 CU A:CU201 0.0 7.3 0.5 CU A:CU201 1.1 13.4 0.3 OD1 A:ASP2 1.9 13.0 1.0 N A:ASP2 2.0 11.9 1.0 N A:SER1 2.1 13.8 1.0 O A:HOH314 2.6 15.7 1.0 C A:SER1 2.8 13.8 1.0 CG A:ASP2 2.9 12.2 1.0 CA A:SER1 3.0 15.0 1.0 CA A:ASP2 3.0 11.8 1.0 CB A:ASP2 3.2 12.2 1.0 O A:HOH351 3.3 29.1 1.0 N A:LYS3 3.5 11.3 1.0 C A:ASP2 3.8 11.7 1.0 O A:SER1 4.0 15.4 1.0 OG A:SER1 4.0 22.6 1.0 OD2 A:ASP2 4.0 11.8 1.0 OD1 A:ASP43 4.0 14.0 1.0 CB A:SER1 4.1 19.5 1.0 CG A:ASP43 4.4 12.5 1.0 CA A:LYS3 4.8 12.1 1.0 OD2 A:ASP43 4.8 13.0 1.0 CG A:LYS3 4.8 12.6 1.0 CB A:LYS3 5.0 12.7 1.0 O A:ASP2 5.0 12.7 1.0

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