Calcium in PDB 5a51: The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine
Protein crystallography data
The structure of The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine, PDB code: 5a51
was solved by
M.Diaz,
A.Albert,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.787 /
1.60
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
35.583,
89.769,
109.642,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.23 /
22.17
|
Calcium Binding Sites:
The binding sites of Calcium atom in the The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine
(pdb code 5a51). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the
The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine, PDB code: 5a51:
Jump to Calcium binding site number:
1;
2;
3;
4;
Calcium binding site 1 out
of 4 in 5a51
Go back to
Calcium Binding Sites List in 5a51
Calcium binding site 1 out
of 4 in the The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca1195
b:15.3
occ:1.00
|
OD2
|
A:ASP102
|
2.3
|
15.6
|
1.0
|
O
|
A:HOH2035
|
2.4
|
29.5
|
1.0
|
O
|
A:HOH2034
|
2.5
|
28.1
|
1.0
|
O
|
A:ARG50
|
2.5
|
16.6
|
1.0
|
OD2
|
A:ASP104
|
2.5
|
20.2
|
1.0
|
OD1
|
A:ASP51
|
2.5
|
17.1
|
1.0
|
OD1
|
A:ASP104
|
2.6
|
17.2
|
1.0
|
O
|
A:HOH2161
|
2.7
|
17.0
|
1.0
|
CG
|
A:ASP104
|
2.9
|
16.5
|
1.0
|
C
|
A:ARG50
|
3.4
|
13.1
|
1.0
|
CG
|
A:ASP102
|
3.5
|
10.4
|
1.0
|
CG
|
A:ASP51
|
3.7
|
15.7
|
1.0
|
CA
|
A:CA1196
|
3.8
|
12.1
|
1.0
|
OD2
|
A:ASP110
|
3.9
|
27.3
|
1.0
|
N
|
A:ASP51
|
4.0
|
14.7
|
1.0
|
CA
|
A:ASP51
|
4.1
|
16.5
|
1.0
|
O
|
A:HOH2165
|
4.2
|
20.8
|
1.0
|
CB
|
A:ARG50
|
4.3
|
14.2
|
1.0
|
OD1
|
A:ASP102
|
4.3
|
10.1
|
1.0
|
CB
|
A:ASP104
|
4.4
|
12.0
|
1.0
|
O
|
A:HOH2164
|
4.4
|
26.6
|
1.0
|
CA
|
A:ARG50
|
4.5
|
13.3
|
1.0
|
CB
|
A:ASP51
|
4.5
|
16.9
|
1.0
|
OD2
|
A:ASP51
|
4.5
|
16.8
|
1.0
|
CB
|
A:ASP102
|
4.5
|
10.6
|
1.0
|
CG
|
A:ASP110
|
4.6
|
21.4
|
1.0
|
O
|
A:HOH2036
|
4.6
|
33.5
|
1.0
|
O
|
A:HOH2040
|
4.7
|
15.9
|
1.0
|
O
|
A:ASP102
|
4.9
|
12.3
|
1.0
|
O
|
A:LYS108
|
4.9
|
14.4
|
1.0
|
CB
|
A:ASP110
|
5.0
|
14.9
|
1.0
|
|
Calcium binding site 2 out
of 4 in 5a51
Go back to
Calcium Binding Sites List in 5a51
Calcium binding site 2 out
of 4 in the The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca1196
b:12.1
occ:1.00
|
OD2
|
A:ASP56
|
2.4
|
13.7
|
1.0
|
OD1
|
A:ASP102
|
2.4
|
10.1
|
1.0
|
OD1
|
A:ASP104
|
2.4
|
17.2
|
1.0
|
O
|
A:HIS103
|
2.5
|
9.6
|
1.0
|
O
|
A:HOH2040
|
2.5
|
15.9
|
1.0
|
OD2
|
A:ASP51
|
2.5
|
16.8
|
1.0
|
OD1
|
A:ASP51
|
2.6
|
17.1
|
1.0
|
CG
|
A:ASP51
|
2.9
|
15.7
|
1.0
|
OD2
|
A:ASP102
|
3.0
|
15.6
|
1.0
|
CG
|
A:ASP102
|
3.0
|
10.4
|
1.0
|
CG
|
A:ASP56
|
3.4
|
12.0
|
1.0
|
C
|
A:HIS103
|
3.4
|
10.1
|
1.0
|
CG
|
A:ASP104
|
3.6
|
16.5
|
1.0
|
CA
|
A:CA1195
|
3.8
|
15.3
|
1.0
|
CB
|
A:ASP56
|
3.9
|
10.5
|
1.0
|
CA
|
A:ASP104
|
4.0
|
10.1
|
1.0
|
N
|
A:ASP104
|
4.0
|
8.4
|
1.0
|
N
|
A:ASP56
|
4.1
|
8.4
|
1.0
|
O
|
A:HOH2041
|
4.4
|
21.4
|
1.0
|
N
|
A:HIS103
|
4.4
|
9.9
|
1.0
|
O
|
A:HOH2167
|
4.4
|
18.6
|
1.0
|
CB
|
A:ASP104
|
4.4
|
12.0
|
1.0
|
CB
|
A:ASP51
|
4.4
|
16.9
|
1.0
|
C
|
A:ASP102
|
4.4
|
9.5
|
1.0
|
CB
|
A:ASP102
|
4.5
|
10.6
|
1.0
|
OD1
|
A:ASP56
|
4.5
|
16.0
|
1.0
|
OD2
|
A:ASP104
|
4.5
|
20.2
|
1.0
|
O
|
A:HOH2164
|
4.5
|
26.6
|
1.0
|
CA
|
A:HIS103
|
4.5
|
9.6
|
1.0
|
CA
|
A:ASP56
|
4.6
|
10.3
|
1.0
|
O
|
A:ASP102
|
4.6
|
12.3
|
1.0
|
O
|
A:HOH2161
|
4.7
|
17.0
|
1.0
|
C
|
A:SER55
|
4.8
|
10.3
|
1.0
|
CA
|
A:SER55
|
4.9
|
11.9
|
1.0
|
CA
|
A:ASP102
|
4.9
|
10.7
|
1.0
|
|
Calcium binding site 3 out
of 4 in 5a51
Go back to
Calcium Binding Sites List in 5a51
Calcium binding site 3 out
of 4 in the The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca1195
b:10.1
occ:1.00
|
OD1
|
B:ASP104
|
2.4
|
13.4
|
1.0
|
O
|
B:HIS103
|
2.4
|
11.0
|
1.0
|
OD2
|
B:ASP56
|
2.4
|
11.9
|
1.0
|
OD1
|
B:ASP102
|
2.4
|
9.7
|
1.0
|
O
|
B:HOH2048
|
2.4
|
13.5
|
1.0
|
OD2
|
B:ASP51
|
2.5
|
12.4
|
1.0
|
OD1
|
B:ASP51
|
2.6
|
12.6
|
1.0
|
CG
|
B:ASP51
|
2.9
|
13.2
|
1.0
|
CG
|
B:ASP102
|
3.1
|
8.1
|
1.0
|
OD2
|
B:ASP102
|
3.2
|
10.8
|
1.0
|
C
|
B:HIS103
|
3.4
|
11.7
|
1.0
|
CG
|
B:ASP56
|
3.4
|
12.9
|
1.0
|
CG
|
B:ASP104
|
3.6
|
12.9
|
1.0
|
CA
|
B:CA1196
|
3.8
|
10.1
|
1.0
|
CB
|
B:ASP56
|
4.0
|
10.9
|
1.0
|
CA
|
B:ASP104
|
4.0
|
11.0
|
1.0
|
O
|
B:HOH2047
|
4.1
|
26.0
|
1.0
|
N
|
B:ASP104
|
4.1
|
9.4
|
1.0
|
N
|
B:ASP56
|
4.2
|
9.1
|
1.0
|
O
|
B:HOH2068
|
4.2
|
28.1
|
1.0
|
CB
|
B:ASP104
|
4.4
|
11.3
|
1.0
|
CB
|
B:ASP51
|
4.4
|
13.2
|
1.0
|
C
|
B:ASP102
|
4.4
|
8.9
|
1.0
|
O
|
B:HOH2032
|
4.4
|
26.0
|
1.0
|
N
|
B:HIS103
|
4.4
|
8.3
|
1.0
|
O
|
B:HOH2151
|
4.5
|
21.4
|
1.0
|
OD1
|
B:ASP56
|
4.5
|
16.7
|
1.0
|
OD2
|
B:ASP104
|
4.5
|
13.6
|
1.0
|
CA
|
B:HIS103
|
4.5
|
11.1
|
1.0
|
O
|
B:ASP102
|
4.5
|
8.3
|
1.0
|
CB
|
B:ASP102
|
4.6
|
9.2
|
1.0
|
O
|
B:HOH2049
|
4.6
|
19.0
|
1.0
|
CA
|
B:ASP56
|
4.7
|
10.6
|
1.0
|
C
|
B:SER55
|
4.9
|
12.1
|
1.0
|
CA
|
B:ASP102
|
5.0
|
8.1
|
1.0
|
|
Calcium binding site 4 out
of 4 in 5a51
Go back to
Calcium Binding Sites List in 5a51
Calcium binding site 4 out
of 4 in the The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of The Crystal Structure of Arabidopsis Thaliana CAR4 in Complex with Two Calcium Ions and Phophatidyl Serine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca1196
b:10.1
occ:1.00
|
OD2
|
B:ASP102
|
2.4
|
10.8
|
1.0
|
OD2
|
B:ASP110
|
2.4
|
15.0
|
1.0
|
O
|
B:HOH2042
|
2.4
|
16.1
|
1.0
|
OD1
|
B:ASP51
|
2.5
|
12.6
|
1.0
|
O
|
B:ARG50
|
2.5
|
12.5
|
1.0
|
OD2
|
B:ASP104
|
2.5
|
13.6
|
1.0
|
OD1
|
B:ASP104
|
2.6
|
13.4
|
1.0
|
CG
|
B:ASP104
|
2.9
|
12.9
|
1.0
|
C
|
B:ARG50
|
3.4
|
11.9
|
1.0
|
CG
|
B:ASP110
|
3.5
|
15.0
|
1.0
|
CG
|
B:ASP102
|
3.5
|
8.1
|
1.0
|
CG
|
B:ASP51
|
3.6
|
13.2
|
1.0
|
CA
|
B:CA1195
|
3.8
|
10.1
|
1.0
|
N
|
B:ASP51
|
4.0
|
11.8
|
1.0
|
CA
|
B:ASP51
|
4.0
|
13.8
|
1.0
|
O
|
B:HOH2047
|
4.0
|
26.0
|
1.0
|
CB
|
B:ASP110
|
4.1
|
9.8
|
1.0
|
O
|
B:HOH2041
|
4.2
|
25.2
|
1.0
|
O
|
B:HOH2148
|
4.2
|
20.0
|
1.0
|
OD1
|
B:ASP102
|
4.2
|
9.7
|
1.0
|
CB
|
B:ARG50
|
4.2
|
11.4
|
1.0
|
O
|
B:HOH2149
|
4.3
|
25.7
|
1.0
|
CB
|
B:ASP104
|
4.4
|
11.3
|
1.0
|
CB
|
B:ASP51
|
4.4
|
13.2
|
1.0
|
OD2
|
B:ASP51
|
4.4
|
12.4
|
1.0
|
CA
|
B:ARG50
|
4.4
|
11.9
|
1.0
|
OD1
|
B:ASP110
|
4.5
|
19.7
|
1.0
|
O
|
B:HOH2028
|
4.6
|
28.6
|
1.0
|
CB
|
B:ASP102
|
4.6
|
9.2
|
1.0
|
O
|
B:ASP102
|
4.9
|
8.3
|
1.0
|
O
|
B:HOH2048
|
4.9
|
13.5
|
1.0
|
N
|
B:ASP110
|
5.0
|
8.7
|
1.0
|
|
Reference:
M.Diaz,
M.J.Sanchez-Barrena,
J.M.Gonzalez-Rubio,
L.Rodriguez,
D.Fernandez,
R.Antoni,
C.Yunta,
B.Belda-Palazon,
M.Gonzalez-Guzman,
M.Peirats-Llobet,
M.Menendez,
J.Boskovic,
J.A.Marquez,
P.L.Rodriguez,
A.Albert.
Calcium-Dependent Oligomerization of Car Proteins at Cell Membrane Modulates Aba Signaling. Proc.Natl.Acad.Sci.Usa V. 113 E396 2016.
ISSN: ISSN 0027-8424
PubMed: 26719420
DOI: 10.1073/PNAS.1512779113
Page generated: Sun Jul 14 16:18:55 2024
|