Calcium in PDB 1x35: Recombinant T=3 Capsid of A Site Specific Mutant of Semv Cp
Protein crystallography data
The structure of Recombinant T=3 Capsid of A Site Specific Mutant of Semv Cp, PDB code: 1x35
was solved by
V.Sangita,
G.L.Lokesh,
P.S.Satheshkumar,
V.Saravanan,
C.S.Vijay,
H.S.Savithri,
M.R.Murthy,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
4.10
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
471.500,
330.095,
351.474,
90.00,
131.05,
90.00
|
R / Rfree (%)
|
26.8 /
27
|
Calcium Binding Sites:
The binding sites of Calcium atom in the Recombinant T=3 Capsid of A Site Specific Mutant of Semv Cp
(pdb code 1x35). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the
Recombinant T=3 Capsid of A Site Specific Mutant of Semv Cp, PDB code: 1x35:
Jump to Calcium binding site number:
1;
2;
3;
Calcium binding site 1 out
of 3 in 1x35
Go back to
Calcium Binding Sites List in 1x35
Calcium binding site 1 out
of 3 in the Recombinant T=3 Capsid of A Site Specific Mutant of Semv Cp
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Recombinant T=3 Capsid of A Site Specific Mutant of Semv Cp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca269
b:39.8
occ:1.00
|
OD1
|
B:ASN267
|
2.1
|
27.1
|
1.0
|
OD2
|
A:ASP146
|
2.2
|
80.1
|
1.0
|
OD2
|
A:ASP149
|
2.3
|
31.1
|
1.0
|
O
|
B:TYR207
|
2.3
|
38.4
|
1.0
|
OXT
|
B:ASN268
|
2.6
|
92.0
|
1.0
|
O
|
B:ASN268
|
2.7
|
79.1
|
1.0
|
CG
|
A:ASP146
|
2.9
|
80.1
|
1.0
|
CB
|
A:ASP146
|
3.0
|
80.1
|
1.0
|
CG
|
A:ASP149
|
3.2
|
31.1
|
1.0
|
CG
|
B:ASN267
|
3.2
|
27.1
|
1.0
|
OD1
|
A:ASP149
|
3.4
|
31.1
|
1.0
|
C
|
B:TYR207
|
3.5
|
38.4
|
1.0
|
N
|
B:ASN268
|
3.6
|
79.1
|
1.0
|
ND2
|
B:ASN267
|
3.8
|
27.1
|
1.0
|
C
|
B:ASN268
|
3.8
|
79.1
|
1.0
|
N
|
B:TYR207
|
3.9
|
38.4
|
1.0
|
OD1
|
A:ASP146
|
4.1
|
80.1
|
1.0
|
CA
|
B:TYR207
|
4.1
|
38.4
|
1.0
|
CB
|
B:TYR207
|
4.2
|
44.3
|
1.0
|
O
|
B:SER116
|
4.2
|
13.5
|
1.0
|
CA
|
B:ASN268
|
4.3
|
79.1
|
1.0
|
CB
|
B:ASN267
|
4.4
|
27.1
|
1.0
|
CA
|
B:ASN267
|
4.4
|
42.3
|
1.0
|
C
|
B:ASN267
|
4.4
|
42.3
|
1.0
|
CA
|
A:ASP146
|
4.5
|
41.0
|
1.0
|
CB
|
A:ASP149
|
4.6
|
31.1
|
1.0
|
N
|
B:LYS208
|
4.6
|
26.9
|
1.0
|
C
|
B:PRO206
|
4.7
|
12.6
|
1.0
|
O
|
A:ASP146
|
4.7
|
41.0
|
1.0
|
CA
|
B:LYS208
|
4.8
|
26.9
|
1.0
|
N
|
A:ASP149
|
4.9
|
34.0
|
1.0
|
CA
|
A:ASP149
|
4.9
|
34.0
|
1.0
|
CB
|
B:PRO206
|
4.9
|
95.9
|
1.0
|
|
Calcium binding site 2 out
of 3 in 1x35
Go back to
Calcium Binding Sites List in 1x35
Calcium binding site 2 out
of 3 in the Recombinant T=3 Capsid of A Site Specific Mutant of Semv Cp
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of Recombinant T=3 Capsid of A Site Specific Mutant of Semv Cp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Ca270
b:39.8
occ:1.00
|
OD2
|
B:ASP146
|
2.1
|
42.1
|
1.0
|
OD1
|
C:ASN267
|
2.2
|
50.5
|
1.0
|
O
|
C:TYR207
|
2.4
|
27.9
|
1.0
|
OXT
|
C:ASN268
|
2.4
|
96.9
|
1.0
|
O
|
C:ASN268
|
2.4
|
64.5
|
1.0
|
OD1
|
B:ASP149
|
2.4
|
54.6
|
1.0
|
CG
|
C:ASN267
|
2.9
|
50.5
|
1.0
|
CG
|
B:ASP146
|
3.1
|
42.1
|
1.0
|
ND2
|
C:ASN267
|
3.2
|
50.5
|
1.0
|
CB
|
B:ASP146
|
3.4
|
42.1
|
1.0
|
CG
|
B:ASP149
|
3.4
|
54.6
|
1.0
|
C
|
C:TYR207
|
3.5
|
27.9
|
1.0
|
C
|
C:ASN268
|
3.6
|
64.5
|
1.0
|
N
|
C:ASN268
|
3.6
|
64.5
|
1.0
|
OD2
|
B:ASP149
|
3.6
|
54.6
|
1.0
|
CB
|
C:TYR207
|
4.0
|
43.3
|
1.0
|
CE
|
C:LYS208
|
4.1
|
54.3
|
1.0
|
CB
|
C:ASN267
|
4.1
|
50.5
|
1.0
|
CA
|
C:TYR207
|
4.2
|
27.9
|
1.0
|
N
|
C:TYR207
|
4.2
|
27.9
|
1.0
|
OD1
|
B:ASP146
|
4.2
|
42.1
|
1.0
|
CA
|
C:ASN268
|
4.3
|
64.5
|
1.0
|
C
|
C:ASN267
|
4.3
|
41.8
|
1.0
|
CA
|
C:ASN267
|
4.3
|
41.8
|
1.0
|
O
|
C:SER116
|
4.5
|
26.0
|
1.0
|
N
|
C:LYS208
|
4.6
|
13.2
|
1.0
|
CD1
|
C:TYR207
|
4.7
|
43.3
|
1.0
|
CG
|
C:TYR207
|
4.7
|
43.3
|
1.0
|
CB
|
B:ASP149
|
4.8
|
54.6
|
1.0
|
CA
|
C:LYS208
|
4.8
|
13.2
|
1.0
|
CA
|
B:ASP146
|
4.9
|
25.1
|
1.0
|
C
|
C:PRO206
|
5.0
|
17.4
|
1.0
|
O
|
B:ASP146
|
5.0
|
25.1
|
1.0
|
|
Calcium binding site 3 out
of 3 in 1x35
Go back to
Calcium Binding Sites List in 1x35
Calcium binding site 3 out
of 3 in the Recombinant T=3 Capsid of A Site Specific Mutant of Semv Cp
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of Recombinant T=3 Capsid of A Site Specific Mutant of Semv Cp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca271
b:39.8
occ:1.00
|
OD1
|
A:ASN267
|
2.0
|
30.0
|
1.0
|
OD2
|
C:ASP146
|
2.2
|
37.9
|
1.0
|
OD1
|
C:ASP149
|
2.3
|
29.5
|
1.0
|
O
|
A:TYR207
|
2.3
|
28.9
|
1.0
|
OXT
|
A:ASN268
|
2.4
|
76.1
|
1.0
|
O
|
A:ASN268
|
2.5
|
25.3
|
1.0
|
CG
|
A:ASN267
|
3.0
|
30.0
|
1.0
|
CG
|
C:ASP149
|
3.1
|
29.5
|
1.0
|
CG
|
C:ASP146
|
3.1
|
37.9
|
1.0
|
OD2
|
C:ASP149
|
3.3
|
29.5
|
1.0
|
CB
|
C:ASP146
|
3.4
|
37.9
|
1.0
|
ND2
|
A:ASN267
|
3.5
|
30.0
|
1.0
|
C
|
A:TYR207
|
3.5
|
28.9
|
1.0
|
C
|
A:ASN268
|
3.6
|
25.3
|
1.0
|
N
|
A:ASN268
|
3.7
|
25.3
|
1.0
|
N
|
A:TYR207
|
4.0
|
28.9
|
1.0
|
CA
|
A:TYR207
|
4.1
|
28.9
|
1.0
|
O
|
A:SER116
|
4.2
|
19.4
|
1.0
|
CB
|
A:TYR207
|
4.2
|
43.4
|
1.0
|
CB
|
A:ASN267
|
4.2
|
30.0
|
1.0
|
CD
|
A:LYS208
|
4.3
|
21.6
|
1.0
|
OD1
|
C:ASP146
|
4.3
|
37.9
|
1.0
|
CA
|
A:ASN268
|
4.3
|
25.3
|
1.0
|
CA
|
A:ASN267
|
4.4
|
28.5
|
1.0
|
C
|
A:ASN267
|
4.4
|
28.5
|
1.0
|
CB
|
C:ASP149
|
4.6
|
29.5
|
1.0
|
N
|
A:LYS208
|
4.6
|
21.8
|
1.0
|
NZ
|
A:LYS208
|
4.7
|
21.6
|
1.0
|
C
|
A:PRO206
|
4.8
|
10.1
|
1.0
|
CA
|
A:LYS208
|
4.8
|
21.8
|
1.0
|
CD1
|
A:TYR207
|
4.8
|
43.4
|
1.0
|
CA
|
C:ASP146
|
4.9
|
22.8
|
1.0
|
CE
|
A:LYS208
|
4.9
|
21.6
|
1.0
|
N
|
C:ASP149
|
4.9
|
39.3
|
1.0
|
O
|
C:ASP146
|
4.9
|
22.8
|
1.0
|
CB
|
A:PRO206
|
4.9
|
67.2
|
1.0
|
CA
|
C:ASP149
|
5.0
|
39.3
|
1.0
|
|
Reference:
V.Sangita,
G.L.Lokesh,
P.S.Satheshkumar,
V.Saravanan,
C.S.Vijay,
H.S.Savithri,
M.R.Murthy.
Structural Studies on Recombinant T = 3 Capsids of Sesbania Mosaic Virus Coat Protein Mutants. Acta Crystallogr.,Sect.D V. 61 1402 2005.
ISSN: ISSN 0907-4449
PubMed: 16204893
DOI: 10.1107/S0907444905024029
Page generated: Fri Jul 12 07:26:53 2024
|