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Calcium in PDB 4xzp: Crystal Structure of the N-Terminal Domain of Human Galectin-4

Protein crystallography data

The structure of Crystal Structure of the N-Terminal Domain of Human Galectin-4, PDB code: 4xzp was solved by J.K.Rustiguel, M.C.Nonato, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.73 / 1.48
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 72.550, 72.550, 110.302, 90.00, 90.00, 120.00
R / Rfree (%) 14.8 / 18.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the N-Terminal Domain of Human Galectin-4 (pdb code 4xzp). 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 Crystal Structure of the N-Terminal Domain of Human Galectin-4, PDB code: 4xzp:

Calcium binding site 1 out of 1 in 4xzp

Go back to Calcium Binding Sites List in 4xzp
Calcium binding site 1 out of 1 in the Crystal Structure of the N-Terminal Domain of Human Galectin-4


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the N-Terminal Domain of Human Galectin-4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca201

b:12.5
occ:0.47
O A:PHE68 2.3 16.6 1.0
OD1 A:ASP72 2.3 15.7 1.0
O A:GLY70 2.4 18.0 1.0
C A:PHE68 3.3 14.9 1.0
CG A:ASP72 3.4 16.2 1.0
C A:GLY70 3.6 18.4 1.0
CA A:PHE68 3.9 15.2 1.0
OD2 A:ASP72 3.9 16.4 1.0
N A:ASP72 4.0 15.8 1.0
N A:GLY70 4.1 18.1 1.0
CB A:PHE68 4.3 16.6 1.0
C A:ASP69 4.4 19.1 1.0
CA A:GLY70 4.4 18.1 1.0
C A:TRP71 4.4 17.7 1.0
N A:ASP69 4.4 16.7 1.0
CA A:ASP72 4.5 15.9 1.0
CB A:ASP72 4.5 16.4 1.0
N A:TRP71 4.6 19.0 1.0
CA A:TRP71 4.6 19.0 0.5
CA A:TRP71 4.7 18.9 0.5
CA A:ASP69 4.7 18.5 1.0
O A:ASP69 4.8 20.9 1.0

Reference:

J.K.Rustiguel, R.O.Soares, S.P.Meisburger, K.M.Davis, K.L.Malzbender, N.Ando, M.Dias-Baruffi, M.C.Nonato. Full-Length Model of the Human Galectin-4 and Insights Into Dynamics of Inter-Domain Communication. Sci Rep V. 6 33633 2016.
ISSN: ESSN 2045-2322
PubMed: 27642006
DOI: 10.1038/SREP33633
Page generated: Wed Jul 9 02:59:56 2025

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