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Potassium in PDB 3ugx: Crystal Structure of Visual Arrestin

Protein crystallography data

The structure of Crystal Structure of Visual Arrestin, PDB code: 3ugx was solved by R.Batra-Safferling, J.Granzin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.89 / 2.65
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 168.363, 184.329, 90.404, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 25.3

Other elements in 3ugx:

The structure of Crystal Structure of Visual Arrestin also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Visual Arrestin (pdb code 3ugx). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of Visual Arrestin, PDB code: 3ugx:

Potassium binding site 1 out of 1 in 3ugx

Go back to Potassium Binding Sites List in 3ugx
Potassium binding site 1 out of 1 in the Crystal Structure of Visual Arrestin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Visual Arrestin within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K408

b:88.6
occ:1.00
OE1 D:GLU350 3.5 60.0 1.0
OG C:SER229 3.8 38.4 1.0
OD1 C:ASN271 4.0 50.1 1.0
O C:ASN228 4.2 43.2 1.0
OG C:SER273 4.2 54.3 1.0
OE2 D:GLU350 4.2 57.6 1.0
CD D:GLU350 4.3 64.1 1.0
C C:ASN271 4.3 34.0 1.0
N C:SER272 4.5 21.7 1.0
O C:SER272 4.5 33.8 1.0
C C:ASN228 4.5 33.7 1.0
O C:ASN271 4.5 41.7 1.0
OG1 C:THR227 4.5 46.6 1.0
CA C:SER229 4.6 31.8 1.0
CA C:ASN271 4.6 42.4 1.0
C C:SER272 4.6 37.5 1.0
CB C:SER229 4.7 32.7 1.0
N C:SER229 4.7 31.7 1.0
CA C:SER272 4.8 29.6 1.0
N C:ASN228 4.8 37.5 1.0
CG C:ASN271 4.9 46.9 1.0

Reference:

J.Granzin, A.Cousin, M.Weirauch, R.Schlesinger, G.Buldt, R.Batra-Safferling. Crystal Structure of P44, A Constitutively Active Splice Variant of Visual Arrestin. J.Mol.Biol. V. 416 611 2012.
ISSN: ISSN 0022-2836
PubMed: 22306737
DOI: 10.1016/J.JMB.2012.01.028
Page generated: Mon Aug 12 09:42:02 2024

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