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Sodium in PDB 5v0d: Crystal Structure of Human Exonuclease 1 EXO1 (Wt) in Complex with 5' Flap Dna (F2II)

Protein crystallography data

The structure of Crystal Structure of Human Exonuclease 1 EXO1 (Wt) in Complex with 5' Flap Dna (F2II), PDB code: 5v0d was solved by Y.Shi, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.98 / 2.63
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 72.976, 72.976, 180.612, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 23.7

Other elements in 5v0d:

The structure of Crystal Structure of Human Exonuclease 1 EXO1 (Wt) in Complex with 5' Flap Dna (F2II) also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Human Exonuclease 1 EXO1 (Wt) in Complex with 5' Flap Dna (F2II) (pdb code 5v0d). 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 Human Exonuclease 1 EXO1 (Wt) in Complex with 5' Flap Dna (F2II), PDB code: 5v0d:

Sodium binding site 1 out of 1 in 5v0d

Go back to Sodium Binding Sites List in 5v0d
Sodium binding site 1 out of 1 in the Crystal Structure of Human Exonuclease 1 EXO1 (Wt) in Complex with 5' Flap Dna (F2II)


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 Human Exonuclease 1 EXO1 (Wt) in Complex with 5' Flap Dna (F2II) within 5.0Å range:
probe atom residue distance (Å) B Occ
Z:Na403

b:79.4
occ:1.00
O Z:SER222 2.4 73.2 1.0
O A:HOH101 2.4 81.4 1.0
OP2 A:DT4 2.4 0.4 1.0
O Z:HOH547 2.5 78.1 1.0
OG Z:SER229 2.5 81.9 1.0
O Z:ILE233 2.5 84.9 1.0
P A:DT4 3.3 99.8 1.0
OP1 A:DT4 3.3 96.8 1.0
CB Z:SER229 3.4 75.7 1.0
C Z:SER222 3.6 73.6 1.0
C Z:ILE233 3.6 87.7 1.0
CA Z:GLY234 3.9 84.4 1.0
N Z:GLY234 4.2 85.1 1.0
O5' A:DT4 4.3 97.8 1.0
CA Z:SER222 4.4 71.7 1.0
N Z:GLY223 4.5 68.5 1.0
O3' A:DC3 4.6 93.5 1.0
CA Z:GLY223 4.6 70.8 1.0
CA Z:SER229 4.7 72.7 1.0
C3' A:DC3 4.8 95.4 1.0
O Z:HOH542 4.8 90.7 1.0
CA Z:ILE233 4.8 88.4 1.0
O Z:HOH549 4.9 75.8 1.0
C Z:GLY234 5.0 81.4 1.0

Reference:

Y.Shi, H.W.Hellinga, L.S.Beese. Interplay of Catalysis, Fidelity, Threading, and Processivity in the Exo- and Endonucleolytic Reactions of Human Exonuclease I. Proc. Natl. Acad. Sci. V. 114 6010 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28533382
DOI: 10.1073/PNAS.1704845114
Page generated: Tue Oct 8 00:42:19 2024

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