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Calcium in PDB 6jl9: Crystal Structure of A Frog Ependymin Related Protein

Protein crystallography data

The structure of Crystal Structure of A Frog Ependymin Related Protein, PDB code: 6jl9 was solved by S.Y.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 53.01 / 2.00
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 61.208, 61.208, 236.196, 90.00, 90.00, 120.00
R / Rfree (%) 19.4 / 27.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of A Frog Ependymin Related Protein (pdb code 6jl9). 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 A Frog Ependymin Related Protein, PDB code: 6jl9:

Calcium binding site 1 out of 1 in 6jl9

Go back to Calcium Binding Sites List in 6jl9
Calcium binding site 1 out of 1 in the Crystal Structure of A Frog Ependymin Related Protein


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 A Frog Ependymin Related Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca300

b:40.8
occ:1.00
O A:PRO122 2.4 38.0 1.0
O A:HOH407 2.4 39.3 1.0
O A:HOH418 2.4 44.2 1.0
O A:HOH440 2.4 55.7 1.0
O A:HOH410 2.5 41.4 1.0
OD1 A:ASP121 2.5 58.3 1.0
OD2 A:ASP121 2.7 61.2 1.0
CG A:ASP121 2.9 59.4 1.0
C A:PRO122 3.6 37.5 1.0
N A:PRO122 4.2 43.9 1.0
O A:ASP124 4.3 41.0 1.0
C A:ASP121 4.4 43.1 1.0
CB A:ASP121 4.4 58.0 1.0
N A:ASP124 4.4 37.4 1.0
N A:TYR123 4.5 35.5 1.0
CA A:PRO122 4.5 42.2 1.0
CA A:TYR123 4.6 40.6 1.0
CD A:PRO122 4.6 46.3 1.0
OE1 A:GLU175 4.6 38.3 1.0
O A:ASP121 4.6 43.5 1.0
NE1 A:TRP161 4.6 39.9 1.0
OE2 A:GLU175 4.7 42.1 1.0
OD1 A:ASP124 4.8 46.1 1.0
CG A:PRO122 4.8 44.3 1.0
CA A:ASP121 4.8 49.8 1.0
OH A:TYR177 4.9 0.7 1.0

Reference:

J.K.Park, K.Y.Kim, Y.W.Sim, Y.I.Kim, J.K.Kim, C.Lee, J.Han, C.U.Kim, J.E.Lee, S.Park. Structures of Three Ependymin-Related Proteins Suggest Their Function As A Hydrophobic Molecule Binder. Iucrj V. 6 729 2019.
ISSN: ESSN 2052-2525
PubMed: 31316816
DOI: 10.1107/S2052252519007668
Page generated: Tue Jul 16 09:51:45 2024

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