Copper in PDB 1keb: Crystal Structure of Double Mutant M37L,P40S E.Coli Thioredoxin

The structure of Crystal Structure of Double Mutant M37L,P40S E.Coli Thioredoxin, PDB code: 1keb was solved by Rudresh, R.Jain, V.Dani, A.Mitra, S.Srivastava, S.P.Sarma, R.Varadarajan, S.Ramakumar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	29.320, 37.500, 50.740, 69.25, 79.71, 85.39
R / Rfree (%)	18.2 / 22.2

The binding sites of Copper atom in the Crystal Structure of Double Mutant M37L,P40S E.Coli Thioredoxin (pdb code 1keb). 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 Double Mutant M37L,P40S E.Coli Thioredoxin, PDB code: 1keb:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Double Mutant M37L,P40S E.Coli Thioredoxin


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 Double Mutant M37L,P40S E.Coli Thioredoxin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu109 b:20.5 occ:1.00 OD1 A:ASP2 1.9 13.6 1.0 N A:SER1 2.1 19.6 1.0 N A:ASP2 2.1 17.1 1.0 O A:HOH159 2.5 17.6 1.0 C A:SER1 2.9 19.3 1.0 CG A:ASP2 2.9 17.1 1.0 CA A:SER1 2.9 20.1 1.0 CA A:ASP2 3.1 17.6 1.0 CB A:ASP2 3.3 16.3 1.0 OD2 A:ASP43 3.9 17.3 1.0 N A:LYS3 3.9 17.9 1.0 C A:ASP2 4.0 17.1 1.0 OD2 A:ASP2 4.0 18.7 1.0 O A:SER1 4.1 18.8 1.0 CB A:SER1 4.2 20.8 1.0 CG A:ASP43 4.3 19.2 1.0 OG A:SER1 4.4 20.5 1.0 O A:HOH115 4.5 17.0 1.0 OD1 A:ASP43 4.7 20.2 1.0 O A:HOH158 5.0 38.6 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Double Mutant M37L,P40S E.Coli Thioredoxin


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 Double Mutant M37L,P40S E.Coli Thioredoxin within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu109 b:15.1 occ:1.00 OD1 B:ASP2 2.0 13.1 1.0 N B:ASP2 2.0 12.7 1.0 OD1 A:ASP10 2.0 13.2 1.0 N B:SER1 2.0 13.1 1.0 O B:HOH154 2.6 13.3 1.0 CG A:ASP10 2.7 15.1 1.0 C B:SER1 2.8 15.1 1.0 OD2 A:ASP10 2.8 17.1 1.0 CA B:SER1 2.9 14.9 1.0 CG B:ASP2 2.9 12.7 1.0 CA B:ASP2 3.0 12.5 1.0 CB B:ASP2 3.2 13.2 1.0 N B:LYS3 3.7 12.3 1.0 C B:ASP2 3.9 12.9 1.0 OD2 B:ASP43 3.9 18.8 1.0 O B:HOH122 4.0 13.3 1.0 O B:SER1 4.0 15.8 1.0 OD2 B:ASP2 4.1 13.6 1.0 O B:HOH114 4.1 16.0 1.0 O A:HOH175 4.1 30.5 1.0 CB B:SER1 4.2 17.2 1.0 CB A:ASP10 4.2 13.4 1.0 CG B:ASP43 4.3 19.9 1.0 OD1 B:ASP43 4.7 22.6 1.0 OG B:SER1 4.9 23.2 1.0 CB B:ASP43 5.0 17.0 1.0

Rudresh, R.Jain, V.Dani, A.Mitra, S.Srivastava, S.P.Sarma, R.Varadarajan, S.Ramakumar. Structural Consequences of Replacement of An Alpha-Helical Pro Residue in E.Coli Thioredoxin Protein Eng. V. 15 627 2002.
ISSN: ISSN 0269-2139
PubMed: 12364576
DOI: 10.1093/PROTEIN/15.8.627