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Sodium in PDB 2pr5: Structural Basis For Light-Dependent Signaling in the Dimeric Lov Photosensor Ytva (Dark Structure)

Protein crystallography data

The structure of Structural Basis For Light-Dependent Signaling in the Dimeric Lov Photosensor Ytva (Dark Structure), PDB code: 2pr5 was solved by A.Moglich, K.Moffat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.82 / 1.45
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 88.846, 91.634, 34.239, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 22.4

Sodium Binding Sites:

The binding sites of Sodium atom in the Structural Basis For Light-Dependent Signaling in the Dimeric Lov Photosensor Ytva (Dark Structure) (pdb code 2pr5). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structural Basis For Light-Dependent Signaling in the Dimeric Lov Photosensor Ytva (Dark Structure), PDB code: 2pr5:

Sodium binding site 1 out of 1 in 2pr5

Go back to Sodium Binding Sites List in 2pr5
Sodium binding site 1 out of 1 in the Structural Basis For Light-Dependent Signaling in the Dimeric Lov Photosensor Ytva (Dark Structure)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structural Basis For Light-Dependent Signaling in the Dimeric Lov Photosensor Ytva (Dark Structure) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na701

b:22.9
occ:1.00
O A:HOH728 2.7 13.7 1.0
O A:HOH724 2.7 15.0 1.0
O A:HOH706 2.8 25.9 1.0
O A:HOH711 3.8 17.0 1.0
O A:HOH825 3.9 20.6 1.0
CG1 A:VAL75 4.1 14.8 1.0
O A:HOH745 4.2 17.0 1.0
NH1 A:ARG79 4.3 17.8 1.0
O3P A:FMN500 4.3 16.7 1.0
O A:HOH844 4.3 15.2 1.0
O A:HOH889 4.4 32.5 1.0
OE1 A:GLN66 4.5 16.5 1.0
O1P A:FMN500 4.6 14.0 1.0
CB A:VAL75 4.9 14.5 1.0
CG2 A:VAL75 5.0 16.3 1.0

Reference:

A.Moglich, K.Moffat. Structural Basis For Light-Dependent Signaling in the Dimeric Lov Domain of the Photosensor Ytva. J.Mol.Biol. V. 373 112 2007.
ISSN: ISSN 0022-2836
PubMed: 17764689
DOI: 10.1016/J.JMB.2007.07.039
Page generated: Tue Dec 15 05:54:11 2020

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