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Sodium in PDB 3n7z: Crystal Structure of Acetyltransferase From Bacillus Anthracis

Protein crystallography data

The structure of Crystal Structure of Acetyltransferase From Bacillus Anthracis, PDB code: 3n7z was solved by C.Chang, R.Wu, P.Gornicki, R.Zhang, A.Joachimiak, Midwest Center Forstructural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 79.429, 176.859, 109.973, 90.00, 105.73, 90.00
R / Rfree (%) 18.7 / 24.2

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Acetyltransferase From Bacillus Anthracis (pdb code 3n7z). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 6 binding sites of Sodium where determined in the Crystal Structure of Acetyltransferase From Bacillus Anthracis, PDB code: 3n7z:
Jump to Sodium binding site number: 1; 2; 3; 4; 5; 6;

Sodium binding site 1 out of 6 in 3n7z

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Sodium binding site 1 out of 6 in the Crystal Structure of Acetyltransferase From Bacillus Anthracis


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 Acetyltransferase From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na401

b:43.9
occ:1.00
O A:HOH407 2.2 87.6 1.0
OE1 A:GLU227 2.4 28.7 1.0
O A:TYR387 2.7 3.6 1.0
CD A:GLU227 3.5 29.2 1.0
CG A:GLU227 3.9 27.9 1.0
C A:TYR387 3.9 3.4 1.0
O A:GLU226 4.2 28.0 1.0
OE1 A:GLU226 4.2 33.5 1.0
NH2 A:ARG185 4.6 19.1 1.0
CD1 A:TYR387 4.6 3.5 1.0
OE2 A:GLU227 4.6 30.0 1.0
CB A:GLU226 4.8 28.7 1.0
CA A:ASP388 4.8 3.4 1.0
CA A:TYR387 4.8 3.3 1.0
N A:ASP388 4.8 3.5 1.0
CB A:TYR387 4.8 3.2 1.0
C A:GLU226 4.9 28.1 1.0
CG A:TYR387 4.9 3.4 1.0

Sodium binding site 2 out of 6 in 3n7z

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Sodium binding site 2 out of 6 in the Crystal Structure of Acetyltransferase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of Acetyltransferase From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na401

b:49.9
occ:1.00
O B:TYR387 2.5 12.5 1.0
O B:HOH405 2.8 55.0 1.0
OE1 B:GLU227 3.1 33.6 1.0
C B:TYR387 3.7 12.3 1.0
CG B:GLU227 4.0 29.9 1.0
CD B:GLU227 4.0 32.0 1.0
OE1 B:GLU226 4.1 40.4 1.0
CB B:TYR387 4.3 11.9 1.0
CD1 B:TYR387 4.3 9.3 1.0
CA B:TYR387 4.4 11.9 1.0
O B:GLU226 4.5 29.8 1.0
NH2 B:ARG185 4.6 23.4 1.0
N B:ASP388 4.7 12.5 1.0
CG B:TYR387 4.7 10.7 1.0
CA B:ASP388 4.7 12.7 1.0
CB B:GLU226 4.9 30.6 1.0

Sodium binding site 3 out of 6 in 3n7z

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Sodium binding site 3 out of 6 in the Crystal Structure of Acetyltransferase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of Crystal Structure of Acetyltransferase From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Na401

b:48.2
occ:1.00
O C:HOH404 2.1 28.2 1.0
O C:TYR387 2.2 3.9 1.0
OE1 C:GLU227 2.9 29.8 1.0
C C:TYR387 3.4 3.7 1.0
CD C:GLU227 3.9 29.7 1.0
CG C:GLU227 4.0 28.7 1.0
O C:GLU226 4.3 28.4 1.0
N C:ASP388 4.3 3.5 1.0
CD1 C:TYR387 4.4 2.5 1.0
CA C:TYR387 4.4 3.6 1.0
CA C:ASP388 4.4 3.5 1.0
CB C:TYR387 4.6 3.3 1.0
OE1 C:GLU226 4.6 33.8 1.0
CG C:TYR387 4.8 2.9 1.0
NH2 C:ARG185 4.8 23.0 1.0
C C:ASP388 4.9 3.5 1.0
CB C:GLU226 4.9 28.2 1.0
C C:GLU226 5.0 28.0 1.0

Sodium binding site 4 out of 6 in 3n7z

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Sodium binding site 4 out of 6 in the Crystal Structure of Acetyltransferase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 4 of Crystal Structure of Acetyltransferase From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na401

b:43.5
occ:1.00
O D:TYR387 2.6 5.0 1.0
OE1 D:GLU227 2.6 33.5 1.0
O D:HOH405 3.0 42.3 1.0
CD D:GLU227 3.7 33.1 1.0
C D:TYR387 3.8 4.7 1.0
OE1 D:GLU226 3.9 38.7 1.0
CG D:GLU227 4.0 31.1 1.0
NH2 D:ARG185 4.5 23.1 1.0
CA D:ASP388 4.6 4.7 1.0
CD1 D:TYR387 4.6 4.5 1.0
N D:ASP388 4.6 4.6 1.0
O D:GLU226 4.7 31.0 1.0
CB D:TYR387 4.7 4.6 1.0
CA D:TYR387 4.7 4.5 1.0
O D:HOH397 4.8 64.0 1.0
OE2 D:GLU227 4.8 33.8 1.0
CB D:GLU226 4.8 30.5 1.0
CG D:TYR387 5.0 4.8 1.0

Sodium binding site 5 out of 6 in 3n7z

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Sodium binding site 5 out of 6 in the Crystal Structure of Acetyltransferase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 5 of Crystal Structure of Acetyltransferase From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Na401

b:39.1
occ:1.00
O E:HOH402 2.2 33.8 1.0
O E:TYR387 2.4 3.7 1.0
OE1 E:GLU227 2.7 24.1 1.0
OE1 E:GLU226 3.5 36.7 1.0
C E:TYR387 3.7 3.9 1.0
CD E:GLU227 3.8 24.2 1.0
CG E:GLU227 4.1 24.3 1.0
NH2 E:ARG185 4.4 20.7 1.0
CA E:ASP388 4.5 3.8 1.0
N E:ASP388 4.5 3.8 1.0
CD E:GLU226 4.6 35.2 1.0
CA E:TYR387 4.7 3.8 1.0
CD1 E:TYR387 4.7 3.8 1.0
O E:GLU226 4.7 26.3 1.0
CB E:TYR387 4.8 3.6 1.0
OE2 E:GLU227 4.9 23.8 1.0
CB E:GLU226 4.9 27.0 1.0

Sodium binding site 6 out of 6 in 3n7z

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Sodium binding site 6 out of 6 in the Crystal Structure of Acetyltransferase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 6 of Crystal Structure of Acetyltransferase From Bacillus Anthracis within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Na401

b:40.3
occ:1.00
O F:TYR387 2.2 14.5 1.0
O F:HOH404 2.5 45.1 1.0
OE1 F:GLU227 3.0 29.5 1.0
C F:TYR387 3.4 14.4 1.0
CD F:GLU227 4.0 29.0 1.0
CA F:ASP388 4.2 14.3 1.0
N F:ASP388 4.3 14.5 1.0
CG F:GLU227 4.4 28.7 1.0
OE1 F:GLU226 4.4 37.8 1.0
CA F:TYR387 4.5 14.1 1.0
CD1 F:TYR387 4.5 15.1 1.0
CB F:TYR387 4.6 14.0 1.0
NH2 F:ARG185 4.6 25.1 1.0
C F:ASP388 4.7 13.9 1.0
O F:GLU226 4.9 29.2 1.0
CG F:TYR387 4.9 14.4 1.0

Reference:

K.D.Green, T.Biswas, C.Chang, R.Wu, W.Chen, B.K.Janes, D.Chalupska, P.Gornicki, P.C.Hanna, O.V.Tsodikov, A.Joachimiak, S.Garneau-Tsodikova. Biochemical and Structural Analysis of An Eis Family Aminoglycoside Acetyltransferase From Bacillus Anthracis. Biochemistry V. 54 3197 2015.
ISSN: ISSN 0006-2960
PubMed: 25928210
DOI: 10.1021/ACS.BIOCHEM.5B00244
Page generated: Tue Dec 15 06:18:40 2020

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