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Calcium in PDB 1z7s: The Crystal Structure of Coxsackievirus A21

Protein crystallography data

The structure of The Crystal Structure of Coxsackievirus A21, PDB code: 1z7s was solved by C.Xiao, C.M.Bator-Kelly, E.Rieder, P.R.Chipman, A.Craig, R.J.Kuhn, E.Wimmer, M.G.Rossmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.72 / 3.20
Space group P 42 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 348.014, 348.014, 348.014, 90.00, 90.00, 90.00
R / Rfree (%) 22.4 / 23.5

Calcium Binding Sites:

The binding sites of Calcium atom in the The Crystal Structure of Coxsackievirus A21 (pdb code 1z7s). 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 The Crystal Structure of Coxsackievirus A21, PDB code: 1z7s:

Calcium binding site 1 out of 1 in 1z7s

Go back to Calcium Binding Sites List in 1z7s
Calcium binding site 1 out of 1 in the The Crystal Structure of Coxsackievirus A21


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 Coxsackievirus A21 within 5.0Å range:
probe atom residue distance (Å) B Occ
1:Ca299

b:58.4
occ:1.00
OG 1:SER21 2.7 55.9 1.0
OG 1:SER24 2.9 43.8 1.0
O 1:THR22 3.2 46.9 1.0
O 1:ASN63 3.3 44.7 1.0
N 1:SER24 3.4 43.2 1.0
CB 1:SER24 3.6 42.9 1.0
CB 1:SER21 3.8 53.9 1.0
C 1:THR22 3.8 46.8 1.0
C 1:GLN23 3.9 43.6 1.0
CA 1:SER24 4.0 43.5 1.0
O 1:SER21 4.1 50.9 1.0
CB 1:ASN63 4.1 44.2 1.0
C 1:SER21 4.2 51.1 1.0
CA 1:GLN23 4.2 44.6 1.0
C 1:ASN63 4.3 44.4 1.0
N 1:GLN23 4.3 45.5 1.0
N 1:THR22 4.5 49.5 1.0
N 1:ASN63 4.5 40.0 1.0
CA 1:ASN63 4.5 42.8 1.0
CA 1:SER21 4.6 52.9 1.0
O 1:GLN23 4.6 43.1 1.0
CA 1:THR22 4.8 48.2 1.0

Reference:

C.Xiao, C.M.Bator-Kelly, E.Rieder, P.R.Chipman, A.Craig, R.J.Kuhn, E.Wimmer, M.G.Rossmann. The Crystal Structure of Coxsackievirus A21 and Its Interaction with Icam-1. Structure V. 13 1019 2005.
ISSN: ISSN 0969-2126
PubMed: 16004874
DOI: 10.1016/J.STR.2005.04.011
Page generated: Sat Dec 12 03:29:52 2020

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