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Calcium in PDB 5cxf: Crystal Structure of the Extracellular Domain of Glycoprotein B From Human Cytomegalovirus

Protein crystallography data

The structure of Crystal Structure of the Extracellular Domain of Glycoprotein B From Human Cytomegalovirus, PDB code: 5cxf was solved by H.G.Burke, E.E.Heldwein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 57.63 / 3.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 92.183, 133.930, 295.376, 90.00, 90.00, 90.00
R / Rfree (%) 23.2 / 26.9

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Extracellular Domain of Glycoprotein B From Human Cytomegalovirus (pdb code 5cxf). 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 Extracellular Domain of Glycoprotein B From Human Cytomegalovirus, PDB code: 5cxf:

Calcium binding site 1 out of 1 in 5cxf

Go back to Calcium Binding Sites List in 5cxf
Calcium binding site 1 out of 1 in the Crystal Structure of the Extracellular Domain of Glycoprotein B From Human Cytomegalovirus


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 Extracellular Domain of Glycoprotein B From Human Cytomegalovirus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca812

b:94.7
occ:1.00
OD2 C:ASP508 2.4 88.4 1.0
OD2 B:ASP508 2.4 94.4 1.0
OD1 A:ASP508 2.4 81.6 1.0
OD2 A:ASP508 2.4 92.0 1.0
OD1 B:ASP508 2.4 93.1 1.0
CG B:ASP508 2.7 93.1 1.0
CG A:ASP508 2.8 86.0 1.0
CG C:ASP508 3.5 83.8 1.0
OD1 C:ASP508 4.0 82.2 1.0
OG1 A:THR512 4.2 79.9 1.0
CB B:ASP508 4.3 80.2 1.0
CB A:ASP508 4.3 76.7 1.0
OG1 B:THR512 4.6 86.5 1.0
OG1 C:THR512 4.6 83.8 1.0
NE2 A:GLN509 4.7 78.8 1.0
O A:ASP508 4.8 80.1 1.0
CB C:ASP508 4.8 74.1 1.0

Reference:

H.G.Burke, E.E.Heldwein. Crystal Structure of the Human Cytomegalovirus Glycoprotein B. Plos Pathog. V. 11 05227 2015.
ISSN: ESSN 1553-7374
PubMed: 26484870
DOI: 10.1371/JOURNAL.PPAT.1005227
Page generated: Wed Jul 9 04:49:57 2025

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