Cadmium in PDB 1rp4: Structure of ERO1P, Source of Disulfide Bonds For Oxidative Protein Folding in the Cell

The structure of Structure of ERO1P, Source of Disulfide Bonds For Oxidative Protein Folding in the Cell, PDB code: 1rp4 was solved by E.Gross, D.B.Kastner, C.A.Kaiser, D.Fass, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.20
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	73.470, 134.330, 102.680, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 24.4

The binding sites of Cadmium atom in the Structure of ERO1P, Source of Disulfide Bonds For Oxidative Protein Folding in the Cell (pdb code 1rp4). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 2 binding sites of Cadmium where determined in the Structure of ERO1P, Source of Disulfide Bonds For Oxidative Protein Folding in the Cell, PDB code: 1rp4:
Jump to Cadmium binding site number: 1; 2;

Cadmium binding site 1 out of 2 in the Structure of ERO1P, Source of Disulfide Bonds For Oxidative Protein Folding in the Cell


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Structure of ERO1P, Source of Disulfide Bonds For Oxidative Protein Folding in the Cell within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd801 b:44.6 occ:1.00 ND1 A:HIS386 2.3 32.2 1.0 O A:HOH832 2.7 32.0 1.0 CE1 A:HIS386 3.0 32.8 1.0 CG A:HIS386 3.5 31.0 1.0 CB A:HIS386 3.9 34.5 1.0 CA A:HIS386 3.9 36.4 1.0 O A:HIS386 4.0 40.1 1.0 NE2 A:HIS386 4.3 33.4 1.0 OD2 A:ASP147 4.3 51.2 1.0 C A:HIS386 4.4 38.1 1.0 CD2 A:HIS386 4.5 32.3 1.0 NE2 A:GLN385 4.8 54.1 1.0

Cadmium binding site 2 out of 2 in the Structure of ERO1P, Source of Disulfide Bonds For Oxidative Protein Folding in the Cell


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of Structure of ERO1P, Source of Disulfide Bonds For Oxidative Protein Folding in the Cell within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd802 b:89.6 occ:1.00 OE2 A:GLU408 2.7 57.4 1.0 O A:HOH886 3.0 68.3 1.0 OE1 A:GLU408 3.3 56.1 1.0 CD A:GLU408 3.4 54.2 1.0 OE1 A:GLU241 3.4 61.8 1.0 CG A:GLU241 3.5 54.0 1.0 O A:HOH845 3.5 66.2 1.0 NZ A:LYS240 3.6 59.2 1.0 O A:GLU186 3.9 47.2 1.0 CD A:GLU241 3.9 58.4 1.0 NH1 A:ARG405 4.0 49.7 1.0 ND1 A:HIS237 4.2 50.9 1.0 CD A:LYS240 4.3 57.9 1.0 CE A:LYS240 4.6 59.2 1.0 CE1 A:HIS237 4.7 49.8 1.0 CB A:PRO185 4.9 49.8 1.0 CG A:GLU408 4.9 48.4 1.0 CB A:GLU241 4.9 50.5 1.0

E.Gross, D.B.Kastner, C.A.Kaiser, D.Fass. Structure of ERO1P, Source of Disulfide Bonds For Oxidative Protein Folding in the Cell. Cell(Cambridge,Mass.) V. 117 601 2004.
ISSN: ISSN 0092-8674
PubMed: 15163408
DOI: 10.1016/S0092-8674(04)00418-0