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Calcium in PDB 1x36: T=1 Capsid of An Amino-Terminal Deletion Mutant of Semv Cp

Protein crystallography data

The structure of T=1 Capsid of An Amino-Terminal Deletion Mutant of Semv Cp, PDB code: 1x36 was solved by V.Sangita, P.S.Satheshkumar, 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 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 193.451, 313.506, 321.173, 90.00, 90.00, 90.00
R / Rfree (%) 24.5 / 24.7

Calcium Binding Sites:

The binding sites of Calcium atom in the T=1 Capsid of An Amino-Terminal Deletion Mutant of Semv Cp (pdb code 1x36). 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 T=1 Capsid of An Amino-Terminal Deletion Mutant of Semv Cp, PDB code: 1x36:

Calcium binding site 1 out of 1 in 1x36

Go back to Calcium Binding Sites List in 1x36
Calcium binding site 1 out of 1 in the T=1 Capsid of An Amino-Terminal Deletion 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 T=1 Capsid of An Amino-Terminal Deletion Mutant of Semv Cp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca269

b:11.7
occ:1.00
O A:ASN268 2.3 12.8 1.0
O A:TYR207 2.3 10.6 1.0
OD1 A:ASN267 2.3 11.9 1.0
O A:HOH415 2.4 11.3 1.0
C A:ASN268 3.5 13.2 1.0
CG A:ASN267 3.5 12.5 1.0
C A:TYR207 3.5 10.7 1.0
N A:ASN268 3.5 11.6 1.0
CE A:LYS208 3.9 10.3 1.0
CA A:ASN268 4.1 12.4 1.0
C A:ASN267 4.1 12.2 1.0
ND2 A:ASN267 4.3 11.9 1.0
N A:TYR207 4.3 9.5 1.0
CA A:ASN267 4.3 11.8 1.0
CA A:TYR207 4.3 9.8 1.0
NZ A:LYS208 4.3 9.7 1.0
OXT A:ASN268 4.4 13.2 1.0
CB A:TYR207 4.5 8.7 1.0
N A:LYS208 4.5 10.3 1.0
CB A:ASN267 4.5 11.6 1.0
CA A:LYS208 4.6 10.2 1.0
CD1 A:TYR207 4.6 10.2 1.0
O A:SER116 4.7 9.9 1.0
O A:ASN267 5.0 13.6 1.0

Reference:

V.Sangita, P.S.Satheshkumar, H.S.Savithri, M.R.Murthy. Structure of A Mutant T=1 Capsid of Sesbania Mosaic Virus: Role of Water Molecules in Capsid Architecture and Integrity. Acta Crystallogr.,Sect.D V. 61 1406 2005.
ISSN: ISSN 0907-4449
PubMed: 16204894
DOI: 10.1107/S0907444905024030
Page generated: Fri Jul 12 07:27:01 2024

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