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Sodium in PDB 5oxn: Peptst in Complex with Dipeptide Phe-Ala

Protein crystallography data

The structure of Peptst in Complex with Dipeptide Phe-Ala, PDB code: 5oxn was solved by M.Martinez Molledo, E.M.Quistgaard, C.Loew, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.81 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 100.800, 107.900, 109.800, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 21.4

Sodium Binding Sites:

The binding sites of Sodium atom in the Peptst in Complex with Dipeptide Phe-Ala (pdb code 5oxn). 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 Peptst in Complex with Dipeptide Phe-Ala, PDB code: 5oxn:

Sodium binding site 1 out of 1 in 5oxn

Go back to Sodium Binding Sites List in 5oxn
Sodium binding site 1 out of 1 in the Peptst in Complex with Dipeptide Phe-Ala


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Peptst in Complex with Dipeptide Phe-Ala within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na503

b:80.8
occ:1.00
O A:HOH640 2.3 48.4 1.0
O A:HOH670 2.3 76.3 1.0
O A:SER316 2.3 64.0 1.0
O A:PHE319 2.6 49.0 1.0
C A:SER316 3.4 56.4 1.0
C A:PHE319 3.6 47.4 1.0
OG A:SER316 3.8 77.7 1.0
N A:VAL321 4.0 37.8 1.0
CA A:SER317 4.1 55.0 1.0
CB A:SER316 4.2 68.3 1.0
N A:SER317 4.2 51.5 1.0
C A:SER317 4.2 51.7 1.0
N A:PHE319 4.3 47.6 1.0
CA A:PRO320 4.3 39.5 1.0
N A:PRO320 4.3 46.1 1.0
O A:SER317 4.4 56.6 1.0
OE2 A:GLU171 4.4 66.6 1.0
CA A:SER316 4.4 58.4 1.0
C A:PRO320 4.5 40.3 1.0
CA A:PHE319 4.6 49.4 1.0
CB A:VAL321 4.6 42.0 1.0
OE1 A:GLU171 4.7 77.4 1.0
N A:TRP318 4.7 44.1 1.0
CA A:VAL321 4.8 37.8 1.0
CD A:GLU171 5.0 72.9 1.0

Reference:

M.Martinez Molledo, E.M.Quistgaard, A.Flayhan, J.Pieprzyk, C.Low. Multispecific Substrate Recognition in A Proton-Dependent Oligopeptide Transporter. Structure V. 26 467 2018.
ISSN: ISSN 1878-4186
PubMed: 29429879
DOI: 10.1016/J.STR.2018.01.005
Page generated: Tue Dec 15 11:26:07 2020

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