Calcium in PDB 1jhn: Crystal Structure of the Lumenal Domain of Calnexin

The structure of Crystal Structure of the Lumenal Domain of Calnexin, PDB code: 1jhn was solved by J.D.Schrag, J.M.Bergeron, Y.Li, S.Borisova, M.Hahn, D.Y.Thomas, M.Cygler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.80 / 2.90
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	85.772, 85.772, 143.476, 90.00, 90.00, 90.00
R / Rfree (%)	32.7 / 37.7

The binding sites of Calcium atom in the Crystal Structure of the Lumenal Domain of Calnexin (pdb code 1jhn). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of the Lumenal Domain of Calnexin, PDB code: 1jhn:

Calcium binding site 1 out of 1 in the Crystal Structure of the Lumenal Domain of Calnexin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Lumenal Domain of Calnexin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca900 b:70.7 occ:1.00 OD2 A:ASP437 2.2 46.3 1.0 OD1 A:ASP118 2.3 74.8 1.0 O A:SER75 2.3 56.9 1.0 OD1 A:ASP437 2.4 55.8 1.0 CG A:ASP437 2.6 51.3 1.0 CG A:ASP118 3.2 74.8 1.0 O A:LYS119 3.3 54.8 1.0 C A:SER75 3.4 56.3 1.0 OD2 A:ASP118 3.4 74.5 1.0 CA A:SER75 3.9 56.3 1.0 ND2 A:ASN438 3.9 54.1 1.0 CB A:ASP437 4.0 50.0 1.0 N A:ASN438 4.2 52.9 1.0 CB A:SER75 4.3 59.1 1.0 C A:LYS119 4.3 59.7 1.0 N A:PHE76 4.5 58.1 1.0 CB A:PHE76 4.5 59.2 1.0 CB A:ASP118 4.5 74.3 1.0 N A:LYS119 4.7 65.4 1.0 CA A:ASP437 4.7 49.6 1.0 CA A:ASP118 4.7 73.4 1.0 CG A:ASN438 4.8 52.9 1.0 CA A:GLY120 4.8 60.5 1.0 C A:ASP118 4.8 69.0 1.0 CA A:PHE76 4.9 60.7 1.0 C A:PHE76 4.9 64.4 1.0 CD2 A:PHE76 4.9 61.5 1.0

J.D.Schrag, J.J.Bergeron, Y.Li, S.Borisova, M.Hahn, D.Y.Thomas, M.Cygler. The Structure of Calnexin, An Er Chaperone Involved in Quality Control of Protein Folding. Mol.Cell V. 8 633 2001.
ISSN: ISSN 1097-2765
PubMed: 11583625
DOI: 10.1016/S1097-2765(01)00318-5