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Calcium in PDB 2h2t: CD23 Lectin Domain, Calcium 2+-Bound

Protein crystallography data

The structure of CD23 Lectin Domain, Calcium 2+-Bound, PDB code: 2h2t was solved by B.A.Wurzburg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.63 / 1.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.310, 51.261, 58.768, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 20

Calcium Binding Sites:

The binding sites of Calcium atom in the CD23 Lectin Domain, Calcium 2+-Bound (pdb code 2h2t). 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 CD23 Lectin Domain, Calcium 2+-Bound, PDB code: 2h2t:

Calcium binding site 1 out of 1 in 2h2t

Go back to Calcium Binding Sites List in 2h2t
Calcium binding site 1 out of 1 in the CD23 Lectin Domain, Calcium 2+-Bound


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of CD23 Lectin Domain, Calcium 2+-Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca322

b:16.1
occ:1.00
O B:HOH324 2.3 29.3 1.0
O B:HOH323 2.3 22.8 1.0
OD1 B:ASN269 2.4 14.8 1.0
OD2 B:ASP270 2.4 16.3 1.0
O B:ASP270 2.4 16.8 1.0
OE1 B:GLU249 2.5 19.5 1.0
OG1 B:THR251 2.5 19.9 1.0
CD B:GLU249 3.3 17.1 1.0
CG B:ASN269 3.4 14.6 1.0
CG B:ASP270 3.4 17.4 1.0
C B:ASP270 3.5 14.5 1.0
OE2 B:GLU249 3.5 18.9 1.0
N B:ASP270 3.7 12.7 1.0
CB B:THR251 3.8 23.0 1.0
O B:HOH394 4.0 32.9 1.0
CA B:ASP270 4.0 13.5 1.0
N B:THR251 4.0 18.1 1.0
CG2 B:THR251 4.0 24.6 1.0
ND2 B:ASN269 4.1 16.5 1.0
O B:HOH401 4.2 33.7 1.0
OD1 B:ASP270 4.3 20.5 1.0
CB B:ASP270 4.3 16.5 1.0
O B:HOH473 4.4 28.4 1.0
C B:ASN269 4.4 12.5 1.0
CA B:THR251 4.5 20.7 1.0
CB B:ASN269 4.6 12.7 1.0
N B:ALA271 4.6 14.1 1.0
CG B:GLU249 4.7 13.8 1.0
CA B:ASN269 4.7 11.5 1.0

Reference:

B.A.Wurzburg, S.S.Tarchevskaya, T.S.Jardetzky. Structural Changes in the Lectin Domain of CD23, the Low-Affinity Ige Receptor, Upon Calcium Binding. Structure V. 14 1049 2006.
ISSN: ISSN 0969-2126
PubMed: 16765898
DOI: 10.1016/J.STR.2006.03.017
Page generated: Sat Dec 12 03:39:01 2020

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