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Sodium in PDB 3bzl: Crystal Structural of Native Escu C-Terminal Domain

Protein crystallography data

The structure of Crystal Structural of Native Escu C-Terminal Domain, PDB code: 3bzl was solved by R.Zarivach, W.Deng, M.Vuckovic, H.B.Felise, H.V.Nguyen, S.I.Miller, B.B.Finlay, N.C.J.Strynadka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.71
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 102.424, 55.121, 50.257, 90.00, 110.42, 90.00
R / Rfree (%) 18.7 / 21.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structural of Native Escu C-Terminal Domain (pdb code 3bzl). 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 Structural of Native Escu C-Terminal Domain, PDB code: 3bzl:

Sodium binding site 1 out of 1 in 3bzl

Go back to Sodium Binding Sites List in 3bzl
Sodium binding site 1 out of 1 in the Crystal Structural of Native Escu C-Terminal Domain


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structural of Native Escu C-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Na1

b:36.2
occ:1.00
O C:HOH125 2.3 37.4 1.0
O C:HOH114 2.3 35.0 1.0
O C:HOH82 2.4 36.0 1.0
O C:ASN318 2.4 19.1 1.0
O C:HOH46 2.4 43.8 1.0
O C:HOH113 2.5 34.9 1.0
C C:ASN318 3.4 17.4 1.0
CA C:ASN318 3.8 17.1 1.0
NE2 C:GLN323 4.3 24.6 1.0
CD2 C:HIS320 4.4 22.5 0.5
O C:HOH37 4.4 33.8 1.0
OE1 C:GLN323 4.5 24.8 1.0
CB C:ASN318 4.5 17.7 1.0
N C:ILE319 4.6 16.2 1.0
ND2 C:ASN318 4.6 17.5 1.0
NE2 C:HIS320 4.7 23.9 0.5
O C:LYS317 4.8 18.4 1.0
CD C:GLN323 4.9 23.3 1.0
CE1 C:HIS320 4.9 22.6 0.5
ND1 C:HIS320 4.9 21.9 0.5

Reference:

R.Zarivach, W.Deng, M.Vuckovic, H.B.Felise, H.V.Nguyen, S.I.Miller, B.B.Finlay, N.C.Strynadka. Structural Analysis of the Essential Self-Cleaving Type III Secretion Proteins Escu and Spas. Nature V. 453 124 2008.
ISSN: ISSN 0028-0836
PubMed: 18451864
DOI: 10.1038/NATURE06832
Page generated: Tue Dec 15 06:03:49 2020

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