Calcium in PDB 1sav: Human Annexin V with Proline Substitution By Thioproline
Protein crystallography data
The structure of Human Annexin V with Proline Substitution By Thioproline, PDB code: 1sav
was solved by
F.J.Medrano,
C.Minks,
N.Budisa,
R.Huber,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
8.00 /
2.50
|
Space group
|
H 3
|
Cell size a, b, c (Å), α, β, γ (°)
|
99.600,
99.600,
97.040,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
18.6 /
25.9
|
Calcium Binding Sites:
The binding sites of Calcium atom in the Human Annexin V with Proline Substitution By Thioproline
(pdb code 1sav). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 5 binding sites of Calcium where determined in the
Human Annexin V with Proline Substitution By Thioproline, PDB code: 1sav:
Jump to Calcium binding site number:
1;
2;
3;
4;
5;
Calcium binding site 1 out
of 5 in 1sav
Go back to
Calcium Binding Sites List in 1sav
Calcium binding site 1 out
of 5 in the Human Annexin V with Proline Substitution By Thioproline
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Human Annexin V with Proline Substitution By Thioproline within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca321
b:20.9
occ:1.00
|
O
|
A:GLY102
|
2.0
|
30.4
|
1.0
|
OD2
|
A:ASP144
|
2.3
|
44.5
|
1.0
|
O
|
A:GLY104
|
2.4
|
31.6
|
1.0
|
O
|
A:LEU100
|
2.9
|
28.4
|
1.0
|
CG
|
A:ASP144
|
3.1
|
41.4
|
1.0
|
C
|
A:GLY102
|
3.2
|
30.7
|
1.0
|
OD1
|
A:ASP144
|
3.2
|
42.5
|
1.0
|
C
|
A:GLY104
|
3.6
|
29.9
|
1.0
|
N
|
A:GLY104
|
3.7
|
29.0
|
1.0
|
OG1
|
A:THR105
|
3.9
|
27.0
|
1.0
|
C
|
A:ALA103
|
3.9
|
29.2
|
1.0
|
CA
|
A:ALA103
|
4.0
|
29.3
|
1.0
|
N
|
A:ALA103
|
4.0
|
29.8
|
1.0
|
C
|
A:LEU100
|
4.1
|
26.1
|
1.0
|
N
|
A:GLY102
|
4.2
|
30.9
|
1.0
|
CA
|
A:GLY102
|
4.3
|
29.8
|
1.0
|
CA
|
A:GLY104
|
4.3
|
29.4
|
1.0
|
CB
|
A:ASP144
|
4.4
|
35.3
|
1.0
|
C
|
A:LYS101
|
4.5
|
30.7
|
1.0
|
N
|
A:THR105
|
4.6
|
29.9
|
1.0
|
O
|
A:ALA103
|
4.7
|
28.6
|
1.0
|
CA
|
A:THR105
|
4.8
|
28.2
|
1.0
|
O
|
A:LYS101
|
4.8
|
31.3
|
1.0
|
CB
|
A:THR105
|
4.9
|
26.2
|
1.0
|
CA
|
A:LEU100
|
5.0
|
24.5
|
1.0
|
|
Calcium binding site 2 out
of 5 in 1sav
Go back to
Calcium Binding Sites List in 1sav
Calcium binding site 2 out
of 5 in the Human Annexin V with Proline Substitution By Thioproline
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of Human Annexin V with Proline Substitution By Thioproline within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca322
b:23.2
occ:1.00
|
O
|
A:GLY263
|
2.5
|
27.0
|
1.0
|
O
|
A:MET259
|
2.6
|
32.5
|
1.0
|
OD1
|
A:ASP303
|
2.8
|
39.7
|
1.0
|
OD2
|
A:ASP303
|
3.3
|
38.6
|
1.0
|
CG
|
A:ASP303
|
3.4
|
37.5
|
1.0
|
O
|
A:GLY261
|
3.5
|
38.4
|
1.0
|
C
|
A:MET259
|
3.5
|
32.4
|
1.0
|
C
|
A:GLY263
|
3.5
|
27.1
|
1.0
|
OG1
|
A:THR264
|
3.6
|
23.4
|
1.0
|
C
|
A:GLY261
|
4.1
|
36.2
|
1.0
|
CA
|
A:MET259
|
4.2
|
30.3
|
1.0
|
N
|
A:GLY261
|
4.2
|
36.9
|
1.0
|
N
|
A:GLY263
|
4.3
|
33.7
|
1.0
|
CA
|
A:GLY263
|
4.3
|
28.4
|
1.0
|
C
|
A:ALA262
|
4.4
|
34.7
|
1.0
|
N
|
A:THR264
|
4.4
|
26.6
|
1.0
|
O
|
A:ALA262
|
4.5
|
38.4
|
1.0
|
N
|
A:LYS260
|
4.5
|
35.4
|
1.0
|
CA
|
A:THR264
|
4.6
|
23.7
|
1.0
|
C
|
A:LYS260
|
4.6
|
37.9
|
1.0
|
CB
|
A:THR264
|
4.6
|
21.9
|
1.0
|
CA
|
A:GLY261
|
4.7
|
37.0
|
1.0
|
N
|
A:ALA262
|
4.8
|
35.8
|
1.0
|
CA
|
A:LYS260
|
4.8
|
38.0
|
1.0
|
CB
|
A:MET259
|
4.8
|
28.5
|
1.0
|
CB
|
A:ASP303
|
4.9
|
35.4
|
1.0
|
|
Calcium binding site 3 out
of 5 in 1sav
Go back to
Calcium Binding Sites List in 1sav
Calcium binding site 3 out
of 5 in the Human Annexin V with Proline Substitution By Thioproline
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of Human Annexin V with Proline Substitution By Thioproline within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca323
b:24.7
occ:1.00
|
OE1
|
A:GLU72
|
2.1
|
28.9
|
1.0
|
O
|
A:MET28
|
2.6
|
25.5
|
1.0
|
O
|
A:GLY30
|
2.7
|
45.5
|
1.0
|
O
|
A:HOH402
|
2.9
|
43.5
|
1.0
|
O
|
A:GLY32
|
3.0
|
44.8
|
1.0
|
CD
|
A:GLU72
|
3.0
|
28.8
|
1.0
|
OE2
|
A:GLU72
|
3.2
|
30.3
|
1.0
|
OG1
|
A:THR33
|
3.2
|
29.2
|
1.0
|
C
|
A:MET28
|
3.7
|
24.3
|
1.0
|
C
|
A:GLY32
|
3.8
|
42.4
|
1.0
|
C
|
A:GLY30
|
3.9
|
44.0
|
1.0
|
N
|
A:GLY32
|
4.2
|
46.5
|
1.0
|
CB
|
A:THR33
|
4.3
|
33.5
|
1.0
|
CG
|
A:GLU72
|
4.4
|
30.7
|
1.0
|
CA
|
A:THR33
|
4.4
|
34.4
|
1.0
|
N
|
A:THR33
|
4.4
|
38.5
|
1.0
|
CA
|
A:MET28
|
4.4
|
21.9
|
1.0
|
C
|
A:LEU31
|
4.5
|
46.9
|
1.0
|
C
|
A:LYS29
|
4.5
|
35.7
|
1.0
|
N
|
A:GLY30
|
4.6
|
38.3
|
1.0
|
CA
|
A:GLY32
|
4.6
|
44.4
|
1.0
|
O
|
A:LYS29
|
4.7
|
34.7
|
1.0
|
N
|
A:LYS29
|
4.7
|
28.6
|
1.0
|
CA
|
A:GLY30
|
4.8
|
41.7
|
1.0
|
N
|
A:LEU31
|
4.8
|
46.0
|
1.0
|
CA
|
A:LEU31
|
4.8
|
46.4
|
1.0
|
CG2
|
A:THR33
|
4.8
|
29.5
|
1.0
|
|
Calcium binding site 4 out
of 5 in 1sav
Go back to
Calcium Binding Sites List in 1sav
Calcium binding site 4 out
of 5 in the Human Annexin V with Proline Substitution By Thioproline
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of Human Annexin V with Proline Substitution By Thioproline within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca324
b:26.0
occ:1.00
|
O
|
A:HOH457
|
2.9
|
33.6
|
1.0
|
O
|
A:THR33
|
3.5
|
38.0
|
1.0
|
OE1
|
A:GLU35
|
3.5
|
27.5
|
1.0
|
OE2
|
A:GLU35
|
3.7
|
26.2
|
1.0
|
CD
|
A:GLU35
|
4.1
|
25.9
|
1.0
|
N
|
A:THR33
|
4.3
|
38.5
|
1.0
|
O
|
A:HOH458
|
4.6
|
61.7
|
1.0
|
C
|
A:THR33
|
4.6
|
34.8
|
1.0
|
CA
|
A:THR33
|
5.0
|
34.4
|
1.0
|
|
Calcium binding site 5 out
of 5 in 1sav
Go back to
Calcium Binding Sites List in 1sav
Calcium binding site 5 out
of 5 in the Human Annexin V with Proline Substitution By Thioproline
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 5 of Human Annexin V with Proline Substitution By Thioproline within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca325
b:24.6
occ:1.00
|
O
|
A:LEU73
|
3.0
|
29.9
|
1.0
|
O
|
A:LYS70
|
3.2
|
25.7
|
1.0
|
O
|
A:SER71
|
3.3
|
30.7
|
1.0
|
O
|
A:HOH474
|
3.3
|
56.3
|
1.0
|
C
|
A:SER71
|
3.8
|
25.3
|
1.0
|
C
|
A:LEU73
|
4.1
|
27.1
|
1.0
|
CA
|
A:SER71
|
4.1
|
25.0
|
1.0
|
O
|
A:HOH476
|
4.2
|
58.0
|
1.0
|
C
|
A:LYS70
|
4.3
|
22.8
|
1.0
|
CB
|
A:THR74
|
4.4
|
30.0
|
1.0
|
N
|
A:GLU72
|
4.5
|
25.8
|
1.0
|
C
|
A:GLU72
|
4.6
|
27.6
|
1.0
|
O
|
A:GLU72
|
4.7
|
31.0
|
1.0
|
N
|
A:LEU73
|
4.7
|
27.7
|
1.0
|
N
|
A:SER71
|
4.8
|
23.3
|
1.0
|
CA
|
A:THR74
|
4.8
|
27.5
|
1.0
|
N
|
A:THR74
|
4.9
|
27.1
|
1.0
|
CA
|
A:GLU72
|
5.0
|
26.6
|
1.0
|
OG1
|
A:THR74
|
5.0
|
34.0
|
1.0
|
OE1
|
A:GLU78
|
5.0
|
33.8
|
1.0
|
|
Reference:
R.Huber,
R.Berendes,
A.Burger,
M.Schneider,
A.Karshikov,
H.Luecke,
J.Romisch,
E.Paques.
Crystal and Molecular Structure of Human Annexin V After Refinement. Implications For Structure, Membrane Binding and Ion Channel Formation of the Annexin Family of Proteins. J.Mol.Biol. V. 223 683 1992.
ISSN: ISSN 0022-2836
PubMed: 1311770
DOI: 10.1016/0022-2836(92)90984-R
Page generated: Thu Jul 11 22:30:14 2024
|