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Potassium in PDB 6rnq: Crystal Structure of the Dimerization Domain of GEMIN5 at 1.95 A

Protein crystallography data

The structure of Crystal Structure of the Dimerization Domain of GEMIN5 at 1.95 A, PDB code: 6rnq was solved by M.Moreno-Morcillo, S.Ramon-Maiques, E.Martinez-Salas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.40 / 1.95
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 64.219, 54.972, 103.640, 90.00, 104.30, 90.00
R / Rfree (%) 21.1 / 23.5

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the Dimerization Domain of GEMIN5 at 1.95 A (pdb code 6rnq). 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 the Dimerization Domain of GEMIN5 at 1.95 A, PDB code: 6rnq:

Potassium binding site 1 out of 1 in 6rnq

Go back to Potassium Binding Sites List in 6rnq
Potassium binding site 1 out of 1 in the Crystal Structure of the Dimerization Domain of GEMIN5 at 1.95 A


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 the Dimerization Domain of GEMIN5 at 1.95 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1101

b:0.7
occ:1.00
HB2 A:TYR958 3.6 65.4 1.0
H A:TYR958 3.9 59.5 1.0
CD1 B:TYR958 4.1 45.8 1.0
CE1 B:TYR958 4.1 45.9 1.0
HD1 B:TYR958 4.3 54.9 1.0
HD2 A:TYR958 4.3 69.0 1.0
CG B:TYR958 4.3 45.4 1.0
HE1 B:TYR958 4.4 55.1 1.0
CZ B:TYR958 4.4 46.0 1.0
O A:HOH1132 4.4 61.7 1.0
HA2 A:GLY957 4.5 56.0 1.0
HB2 B:TYR958 4.6 55.5 1.0
CD2 B:TYR958 4.6 46.0 1.0
N A:TYR958 4.6 49.6 1.0
CB A:TYR958 4.6 54.5 1.0
CE2 B:TYR958 4.6 45.7 1.0
O B:HOH1202 4.9 46.4 1.0
HB3 A:TYR958 5.0 65.4 1.0
CB B:TYR958 5.0 46.2 1.0

Reference:

M.Moreno-Morcillo, R.Francisco-Velilla, A.Embarc-Buh, J.Fernandez-Chamorro, S.Ramon-Maiques, E.Martinez-Salas. A Novel GEMIN5 Dimerization Module Is Critical For Protein Recruitment and Translation Control Nucleic Acids Res. 2019.
ISSN: ESSN 1362-4962
Page generated: Mon Aug 12 17:29:45 2024

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