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Sodium in PDB 3rdq: Crystal Structure of R7-2 Streptavidin Complexed with Desthiobiotin

Protein crystallography data

The structure of Crystal Structure of R7-2 Streptavidin Complexed with Desthiobiotin, PDB code: 3rdq was solved by V.N.Malashkevich, M.Magalhaes, C.M.Czecster, R.Guan, M.Levy, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.98 / 1.60
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 57.275, 57.275, 183.742, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 19

Other elements in 3rdq:

The structure of Crystal Structure of R7-2 Streptavidin Complexed with Desthiobiotin also contains other interesting chemical elements:

Nickel (Ni) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of R7-2 Streptavidin Complexed with Desthiobiotin (pdb code 3rdq). 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 Crystal Structure of R7-2 Streptavidin Complexed with Desthiobiotin, PDB code: 3rdq:

Sodium binding site 1 out of 1 in 3rdq

Go back to Sodium Binding Sites List in 3rdq
Sodium binding site 1 out of 1 in the Crystal Structure of R7-2 Streptavidin Complexed with Desthiobiotin


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of R7-2 Streptavidin Complexed with Desthiobiotin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na303

b:22.5
occ:1.00
O A:HOH189 2.4 26.4 1.0
O A:ALA119 2.4 17.8 1.0
OG A:SER122 2.5 18.4 1.0
C A:ALA119 3.4 18.4 1.0
CB A:SER122 3.5 18.5 1.0
CB A:ALA119 4.0 21.2 1.0
CA A:ALA119 4.1 19.9 1.0
O A:HOH148 4.2 17.2 1.0
N A:TRP120 4.4 18.7 1.0
OG1 A:THR123 4.4 17.4 1.0
N A:SER122 4.4 17.0 1.0
CA A:SER122 4.5 16.9 1.0
CA A:TRP120 4.6 17.1 1.0
C A:TRP120 4.9 17.4 1.0

Reference:

M.L.Magalhaes, C.M.Czekster, R.Guan, V.N.Malashkevich, S.C.Almo, M.Levy. Evolved Streptavidin Mutants Reveal Key Role of Loop Residue in High-Affinity Binding. Protein Sci. V. 20 1145 2011.
ISSN: ISSN 0961-8368
PubMed: 21520321
DOI: 10.1002/PRO.642
Page generated: Tue Dec 15 06:23:41 2020

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