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Calcium in PDB 2rhp: The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure

Protein crystallography data

The structure of The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure, PDB code: 2rhp was solved by C.B.Carlson, J.L.Keck, D.F.Mosher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.90
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.892, 122.650, 155.381, 90.00, 90.00, 90.00
R / Rfree (%) 22.7 / 27.7

Calcium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30;

Binding sites:

The binding sites of Calcium atom in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure (pdb code 2rhp). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 30 binding sites of Calcium where determined in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure, PDB code: 2rhp:
Jump to Calcium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Calcium binding site 1 out of 30 in 2rhp

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Calcium binding site 1 out of 30 in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1173

b:18.6
occ:1.00
OD2 A:ASP946 2.2 25.7 1.0
OD2 A:ASP939 2.3 29.2 1.0
O A:ILE954 2.3 25.0 1.0
O A:ASN951 2.4 24.3 1.0
OD2 A:ASP937 2.5 29.4 1.0
O A:CYS948 2.5 27.2 1.0
OD1 A:ASP946 2.6 25.2 1.0
CG A:ASP946 2.7 25.6 1.0
OG A:SER955 2.9 27.2 1.0
CG A:ASP939 3.4 29.3 1.0
C A:ILE954 3.4 25.2 1.0
CG A:ASP937 3.4 29.9 1.0
C A:ASN951 3.4 24.6 1.0
C A:CYS948 3.5 26.8 1.0
OD1 A:ASP937 3.7 29.7 1.0
OD1 A:ASP939 3.8 29.7 1.0
CA A:SER955 3.9 26.9 1.0
CB A:SER955 3.9 26.8 1.0
CA A:CA2 4.0 32.4 1.0
N A:SER955 4.1 26.4 1.0
CB A:ASP946 4.2 25.5 1.0
N A:ASN951 4.2 24.4 1.0
N A:PRO949 4.3 26.1 1.0
N A:ASN952 4.3 24.6 1.0
CA A:ASN952 4.3 24.9 1.0
CA A:ASN951 4.3 24.5 1.0
CA A:CYS948 4.3 26.9 1.0
CA A:PRO949 4.4 26.1 1.0
N A:ILE954 4.4 24.1 1.0
CB A:CYS948 4.4 27.1 1.0
N A:CYS948 4.5 27.0 1.0
CA A:ILE954 4.5 24.5 1.0
CB A:ASP939 4.6 28.7 1.0
C A:PRO949 4.7 26.2 1.0
C A:ASN952 4.7 24.7 1.0
CB A:ASP937 4.7 30.2 1.0
CB A:ASN951 4.8 24.4 1.0
O A:PRO949 5.0 26.7 1.0
N A:ALA953 5.0 24.1 1.0

Calcium binding site 2 out of 30 in 2rhp

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Calcium binding site 2 out of 30 in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure


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Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca2

b:32.4
occ:1.00
OD1 A:ASP937 2.1 29.7 1.0
OD1 A:ASP935 2.2 34.7 1.0
O A:ILE941 2.3 23.7 1.0
OD2 A:ASP946 2.5 25.7 1.0
OD1 A:ASP939 2.7 29.7 1.0
CG A:ASP937 3.1 29.9 1.0
CG A:ASP935 3.5 34.3 1.0
CG A:ASP939 3.5 29.3 1.0
OD2 A:ASP937 3.5 29.4 1.0
C A:ILE941 3.6 24.4 1.0
CG A:ASP946 3.6 25.6 1.0
OD2 A:ASP939 3.7 29.2 1.0
CB A:ASP946 3.9 25.5 1.0
CA A:CA1173 4.0 18.6 1.0
N A:ASP937 4.1 31.0 1.0
O A:PRO949 4.1 26.7 1.0
CA A:ASP935 4.2 33.8 1.0
OD2 A:ASP935 4.3 34.7 1.0
C A:ASP935 4.3 33.0 1.0
N A:ASN938 4.3 30.0 1.0
CB A:ASP937 4.4 30.2 1.0
N A:ASP939 4.4 29.2 1.0
CB A:ASP935 4.4 34.0 1.0
CA A:PRO949 4.4 26.1 1.0
N A:ILE941 4.4 26.0 1.0
CA A:ILE941 4.5 25.2 1.0
N A:PRO942 4.5 24.0 1.0
C A:PRO942 4.5 23.9 1.0
O A:ASP935 4.6 33.5 1.0
CA A:ASP937 4.6 30.4 1.0
CA A:PRO942 4.6 23.8 1.0
N A:PHE936 4.6 31.6 1.0
N A:ASP943 4.6 24.6 1.0
C A:PRO949 4.7 26.2 1.0
OD1 A:ASP946 4.7 25.2 1.0
C A:ASP937 4.7 30.3 1.0
OD1 A:ASP943 4.7 26.4 1.0
CB A:ILE941 4.7 25.5 1.0
O A:PRO942 4.8 23.4 1.0
CB A:ASP939 4.8 28.7 1.0

Calcium binding site 3 out of 30 in 2rhp

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Calcium binding site 3 out of 30 in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca3

b:32.8
occ:1.00
OD1 A:ASP926 2.3 42.6 1.0
OD1 A:ASP924 2.4 42.7 1.0
OD1 A:ASP930 2.4 37.8 1.0
O A:ARG928 2.4 37.6 1.0
OD1 A:ASP922 2.6 38.8 1.0
CG A:ASP926 3.2 42.2 1.0
CG A:ASP930 3.3 37.8 1.0
CG A:ASP924 3.5 42.3 1.0
OD2 A:ASP926 3.5 42.5 1.0
C A:ARG928 3.6 37.9 1.0
O A:HOH1211 3.6 41.4 1.0
CG A:ASP922 3.6 38.8 1.0
N A:ASP930 3.7 36.7 1.0
CA A:ASP930 3.8 36.8 1.0
OD2 A:ASP924 3.9 42.4 1.0
C A:GLY929 4.1 36.7 1.0
OD2 A:ASP930 4.1 37.9 1.0
CB A:ASP930 4.1 37.3 1.0
CA A:ASP922 4.1 39.5 1.0
CB A:ASP922 4.4 39.3 1.0
CA A:ARG928 4.5 38.5 1.0
CB A:ASP926 4.5 41.5 1.0
N A:GLY929 4.5 37.3 1.0
OD2 A:ASP922 4.5 38.3 1.0
C A:ASP922 4.5 39.7 1.0
O A:GLY929 4.5 36.7 1.0
N A:ARG928 4.5 39.0 1.0
CA A:GLY929 4.6 37.0 1.0
N A:ASP926 4.7 41.4 1.0
CB A:ARG928 4.7 38.7 1.0
CB A:ASP924 4.7 41.6 1.0
N A:ASP924 4.7 41.0 1.0
N A:LEU923 4.8 40.0 1.0
O A:GLU921 4.9 40.0 1.0
N A:GLY925 5.0 41.0 1.0

Calcium binding site 4 out of 30 in 2rhp

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Calcium binding site 4 out of 30 in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1174

b:31.2
occ:1.00
OD2 A:ASP910 2.3 35.6 1.0
OD1 A:ASP899 2.3 33.8 1.0
OD1 A:ASP901 2.3 33.5 1.0
OD1 A:ASP903 2.4 34.7 1.0
O A:VAL905 2.4 37.8 1.0
O A:HOH1204 2.5 31.8 1.0
CG A:ASP903 3.0 34.8 1.0
OD2 A:ASP903 3.1 34.4 1.0
CG A:ASP901 3.3 33.6 1.0
CG A:ASP910 3.4 36.2 1.0
CG A:ASP899 3.5 34.0 1.0
OD2 A:ASP901 3.5 33.7 1.0
C A:VAL905 3.6 38.0 1.0
CA A:CA1175 4.0 31.9 1.0
CB A:ASP910 4.0 36.9 1.0
OD2 A:ASP899 4.2 34.0 1.0
O A:ARG913 4.3 35.5 1.0
N A:ASP903 4.3 34.7 1.0
CB A:ASP903 4.3 34.9 1.0
C A:PRO906 4.4 39.7 1.0
O A:PRO906 4.4 39.8 1.0
N A:ASP901 4.4 33.1 1.0
OD1 A:ASP910 4.4 36.4 1.0
CA A:VAL905 4.4 37.5 1.0
OD1 A:ASP907 4.5 40.2 1.0
N A:VAL905 4.5 37.1 1.0
CA A:ASP899 4.6 33.3 1.0
N A:PRO906 4.6 38.6 1.0
CB A:ASP901 4.6 33.5 1.0
N A:ASP900 4.6 32.6 1.0
CB A:VAL905 4.6 37.4 1.0
CB A:ASP899 4.6 33.7 1.0
CA A:PRO906 4.7 39.2 1.0
N A:ASP907 4.7 40.2 1.0
N A:ASN902 4.7 33.9 1.0
CA A:ASP903 4.8 35.1 1.0
C A:ASP899 4.8 33.0 1.0
CA A:ASP901 4.9 33.6 1.0
C A:ARG913 4.9 35.7 1.0
N A:GLY904 5.0 36.0 1.0
CA A:ARG913 5.0 36.4 1.0

Calcium binding site 5 out of 30 in 2rhp

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Calcium binding site 5 out of 30 in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 5 of The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1175

b:31.9
occ:1.00
OD2 A:ASP903 2.1 34.4 1.0
OD1 A:ASN917 2.4 37.4 1.0
O A:CYS912 2.4 36.9 1.0
OD2 A:ASP901 2.5 33.7 1.0
O A:VAL915 2.6 33.9 1.0
OD1 A:ASP910 2.7 36.4 1.0
OD2 A:ASP910 2.7 35.6 1.0
CG A:ASP910 3.1 36.2 1.0
CG A:ASP903 3.4 34.8 1.0
C A:CYS912 3.4 37.0 1.0
CG A:ASN917 3.5 37.5 1.0
C A:VAL915 3.5 34.2 1.0
N A:ASN917 3.6 37.3 1.0
CG A:ASP901 3.6 33.6 1.0
CB A:CYS912 3.8 37.2 1.0
CA A:CYS912 4.0 37.3 1.0
CA A:CA1174 4.0 31.2 1.0
OD1 A:ASP901 4.0 33.5 1.0
O A:ASN917 4.1 38.3 1.0
OD1 A:ASP903 4.1 34.7 1.0
NE2 A:GLN920 4.2 40.4 1.0
C A:PHE916 4.2 36.7 1.0
N A:CYS912 4.2 37.9 1.0
CA A:PHE916 4.2 35.6 1.0
N A:PHE916 4.2 34.8 1.0
CA A:ASN917 4.3 37.9 1.0
CB A:ASN917 4.3 37.6 1.0
CB A:ASP903 4.3 34.9 1.0
N A:ARG913 4.3 36.6 1.0
N A:VAL915 4.4 34.9 1.0
C A:ASN917 4.5 38.4 1.0
ND2 A:ASN917 4.5 37.3 1.0
CA A:VAL915 4.5 34.3 1.0
CB A:ASP910 4.5 36.9 1.0
CA A:ARG913 4.6 36.4 1.0
C A:ARG913 4.6 35.7 1.0
O A:ARG913 4.8 35.5 1.0
CB A:ASP901 4.9 33.5 1.0
N A:LEU914 5.0 35.5 1.0

Calcium binding site 6 out of 30 in 2rhp

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Calcium binding site 6 out of 30 in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 6 of The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1176

b:37.2
occ:1.00
OD2 A:ASP890 2.3 34.8 1.0
OD2 A:ASP897 2.4 33.6 1.0
O A:ASP899 2.4 32.6 1.0
OD1 A:ASN902 2.7 33.7 1.0
OD2 A:ASP888 2.7 32.3 1.0
OD1 A:ASP897 2.9 33.5 1.0
CG A:ASP897 3.0 33.7 1.0
CG A:ASP890 3.5 35.0 1.0
CG A:ASN902 3.5 33.6 1.0
C A:ASP899 3.5 33.0 1.0
CG A:ASP888 3.8 32.2 1.0
ND2 A:ASN902 3.9 32.9 1.0
CA A:CA7 3.9 32.4 1.0
OD1 A:ASP890 4.0 35.0 1.0
CB A:ASP899 4.2 33.7 1.0
CA A:ASP899 4.2 33.3 1.0
OD1 A:ASP888 4.3 32.0 1.0
N A:ASP899 4.4 33.4 1.0
CB A:ASP897 4.5 33.9 1.0
N A:ASP900 4.5 32.6 1.0
CB A:ASP890 4.7 34.6 1.0
N A:ASN902 4.7 33.9 1.0
CB A:ASN902 4.7 33.6 1.0
OE1 A:GLN892 4.7 37.3 1.0
CA A:ASP900 4.7 32.3 1.0
CA A:ASN902 4.8 34.0 1.0
C A:ASP900 4.9 32.6 1.0

Calcium binding site 7 out of 30 in 2rhp

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Calcium binding site 7 out of 30 in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 7 of The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca7

b:32.4
occ:1.00
OD1 A:ASP886 2.3 33.9 1.0
OD1 A:ASP890 2.3 35.0 1.0
O A:GLN892 2.3 34.9 1.0
OD1 A:ASP888 2.3 32.0 1.0
OD2 A:ASP897 2.6 33.6 1.0
CG A:ASP890 3.0 35.0 1.0
CG A:ASP888 3.1 32.2 1.0
OD2 A:ASP890 3.2 34.8 1.0
OD2 A:ASP888 3.2 32.3 1.0
C A:GLN892 3.4 34.9 1.0
CG A:ASP886 3.4 33.3 1.0
CG A:ASP897 3.7 33.7 1.0
CA A:CA1176 3.9 37.2 1.0
N A:GLN892 3.9 34.9 1.0
CA A:GLN892 4.1 35.1 1.0
N A:ASP890 4.1 34.1 1.0
OD1 A:ASP894 4.1 33.2 1.0
OD2 A:ASP886 4.2 33.8 1.0
CB A:ASP897 4.2 33.9 1.0
CB A:GLN892 4.3 35.7 1.0
CB A:ASP890 4.3 34.6 1.0
CA A:ASP886 4.4 32.3 1.0
CB A:ASP886 4.4 32.6 1.0
N A:GLY893 4.5 34.4 1.0
C A:ASP886 4.5 32.3 1.0
CB A:ASP888 4.5 32.3 1.0
N A:ASP894 4.5 33.9 1.0
N A:ASP888 4.5 33.1 1.0
N A:ARG889 4.6 34.0 1.0
CA A:ASP890 4.6 34.4 1.0
N A:GLY891 4.6 34.4 1.0
O A:ASP900 4.7 32.7 1.0
C A:GLY893 4.7 33.7 1.0
O A:ASP886 4.7 32.2 1.0
CA A:GLY893 4.8 33.9 1.0
OD1 A:ASP897 4.8 33.5 1.0
C A:ASP890 4.8 34.7 1.0
O A:ASP899 4.9 32.6 1.0
N A:HIS887 4.9 32.4 1.0
CA A:ASP888 4.9 32.9 1.0
C A:ASP888 5.0 33.1 1.0

Calcium binding site 8 out of 30 in 2rhp

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Calcium binding site 8 out of 30 in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 8 of The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca8

b:36.7
occ:1.00
O A:ASP897 2.1 34.1 1.0
OD2 A:ASP907 2.2 40.5 1.0
O A:ASP894 2.4 34.7 1.0
OD1 A:ASP900 2.4 29.8 1.0
OD2 A:ASP900 2.8 30.5 1.0
O A:HOH1219 2.9 34.4 1.0
CG A:ASP900 2.9 30.6 1.0
C A:ASP897 3.3 34.4 1.0
C A:ASP894 3.4 34.2 1.0
CG A:ASP907 3.4 40.3 1.0
CA A:ASP894 4.0 34.0 1.0
N A:ASP897 4.1 34.5 1.0
CA A:ASP897 4.1 34.2 1.0
OD1 A:ASP907 4.1 40.2 1.0
N A:PRO898 4.3 34.3 1.0
CB A:ASP897 4.3 33.9 1.0
CB A:ASP900 4.4 31.5 1.0
N A:ALA895 4.5 34.5 1.0
CB A:ASP907 4.5 40.4 1.0
CB A:ASP894 4.5 33.7 1.0
CA A:PRO898 4.5 34.1 1.0
CA A:ALA895 4.7 34.9 1.0
C A:PRO898 4.8 33.8 1.0
C A:ALA895 4.8 35.2 1.0
N A:ASP900 4.8 32.6 1.0
CA A:ASP900 4.9 32.3 1.0
N A:ASP899 5.0 33.4 1.0

Calcium binding site 9 out of 30 in 2rhp

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Calcium binding site 9 out of 30 in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 9 of The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca9

b:27.7
occ:1.00
OD2 A:ASP874 2.3 26.2 1.0
OD2 A:ASP865 2.3 32.4 1.0
OD2 A:ASP867 2.3 30.2 1.0
OD1 A:ASN881 2.3 30.8 1.0
O A:ILE879 2.4 31.5 1.0
O A:CYS876 2.4 32.0 1.0
OD1 A:ASP874 2.9 26.1 1.0
CG A:ASP874 2.9 26.4 1.0
C A:ILE879 3.1 31.7 1.0
CG A:ASP865 3.2 32.9 1.0
N A:ASN881 3.4 30.4 1.0
C A:CYS876 3.4 31.8 1.0
CG A:ASP867 3.5 29.7 1.0
CG A:ASN881 3.5 30.5 1.0
OD1 A:ASP865 3.5 33.0 1.0
N A:SER880 3.7 30.9 1.0
CA A:SER880 3.7 30.2 1.0
C A:SER880 3.8 30.3 1.0
CB A:CYS876 3.9 32.5 1.0
CA A:CA10 4.0 25.5 1.0
N A:ILE879 4.0 32.2 1.0
CA A:CYS876 4.1 31.6 1.0
OD1 A:ASP867 4.1 29.4 1.0
CA A:ILE879 4.2 31.9 1.0
NE2 A:GLN884 4.2 28.8 1.0
CA A:ASN881 4.3 30.6 1.0
N A:CYS876 4.3 30.5 1.0
CB A:ASP874 4.3 26.9 1.0
CB A:ASN881 4.4 30.4 1.0
N A:PRO877 4.4 31.8 1.0
O A:PRO877 4.4 31.9 1.0
C A:PRO877 4.4 31.8 1.0
ND2 A:ASN881 4.5 30.2 1.0
O A:ASN881 4.6 31.2 1.0
CA A:PRO877 4.6 31.7 1.0
CB A:ASP867 4.6 29.3 1.0
CB A:ASP865 4.6 33.1 1.0
C A:ASN881 4.7 30.7 1.0
N A:TYR878 4.8 32.1 1.0
O A:SER880 4.8 30.1 1.0
C A:TYR878 4.9 32.7 1.0

Calcium binding site 10 out of 30 in 2rhp

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Calcium binding site 10 out of 30 in the The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 10 of The Thrombospondin-1 Polymorphism ASN700SER Associated with Cornoary Artery Disease Causes Local and Long-Ranging Changes in Protein Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca10

b:25.5
occ:1.00
OD1 A:ASP865 2.2 33.0 1.0
OD1 A:ASP863 2.2 35.7 1.0
O A:HIS869 2.3 27.1 1.0
OD2 A:ASP874 2.4 26.2 1.0
OD1 A:ASP867 2.5 29.4 1.0
CG A:ASP867 3.2 29.7 1.0
CG A:ASP865 3.3 32.9 1.0
CG A:ASP874 3.3 26.4 1.0
CG A:ASP863 3.3 35.8 1.0
OD2 A:ASP867 3.4 30.2 1.0
C A:HIS869 3.5 27.1 1.0
CB A:ASP874 3.7 26.9 1.0
OD2 A:ASP865 3.8 32.4 1.0
CA A:CA9 4.0 27.7 1.0
N A:HIS869 4.1 27.2 1.0
OD2 A:ASP863 4.2 36.1 1.0
CA A:HIS869 4.2 26.9 1.0
O A:PRO877 4.2 31.9 1.0
CB A:ASP863 4.2 35.6 1.0
N A:ASP865 4.3 33.7 1.0
CB A:HIS869 4.3 26.3 1.0
N A:ASP867 4.3 29.9 1.0
OD1 A:ASP874 4.4 26.1 1.0
CA A:ASP863 4.4 35.5 1.0
C A:ASP863 4.5 35.6 1.0
CB A:ASP865 4.5 33.1 1.0
CB A:ASP867 4.6 29.3 1.0
N A:GLN870 4.6 27.6 1.0
N A:ASP866 4.6 32.6 1.0
CA A:ASP865 4.7 33.2 1.0
C A:GLN870 4.7 28.1 1.0
N A:ILE864 4.7 35.1 1.0
C A:ASP865 4.7 33.0 1.0
CA A:GLN870 4.8 28.0 1.0
N A:GLY868 4.8 27.6 1.0
CA A:ASP867 4.9 29.3 1.0
N A:ASN871 4.9 28.3 1.0
O A:ASP863 4.9 35.5 1.0
O A:GLN870 4.9 28.3 1.0
OD1 A:ASN871 4.9 27.9 1.0
C A:PRO877 5.0 31.8 1.0

Reference:

C.B.Carlson, Y.Liu, J.L.Keck, D.F.Mosher. Influences of the N700S Thrombospondin-1 Polymorphism on Protein Structure and Stability. J.Biol.Chem. V. 283 20069 2008.
ISSN: ISSN 0021-9258
PubMed: 18499674
DOI: 10.1074/JBC.M800223200
Page generated: Fri Jul 12 15:56:46 2024

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