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Sodium in PDB 3t90: Crystal Structure of Glucosamine-6-Phosphate N-Acetyltransferase From Arabidopsis Thaliana

Protein crystallography data

The structure of Crystal Structure of Glucosamine-6-Phosphate N-Acetyltransferase From Arabidopsis Thaliana, PDB code: 3t90 was solved by I.Grishkovskaya, T.Herter, H.Riegler, B.Usadel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.88 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 68.520, 47.174, 42.223, 90.00, 100.74, 90.00
R / Rfree (%) 16.5 / 20.1

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Glucosamine-6-Phosphate N-Acetyltransferase From Arabidopsis Thaliana (pdb code 3t90). 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 Glucosamine-6-Phosphate N-Acetyltransferase From Arabidopsis Thaliana, PDB code: 3t90:

Sodium binding site 1 out of 1 in 3t90

Go back to Sodium Binding Sites List in 3t90
Sodium binding site 1 out of 1 in the Crystal Structure of Glucosamine-6-Phosphate N-Acetyltransferase From Arabidopsis Thaliana


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 Glucosamine-6-Phosphate N-Acetyltransferase From Arabidopsis Thaliana within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na151

b:30.8
occ:1.00
O A:HOH284 3.0 39.9 1.0
ND1 A:HIS51 3.4 18.9 1.0
CE1 A:HIS51 3.7 17.7 1.0
CZ A:TYR47 3.7 48.7 1.0
OH A:TYR47 3.8 52.2 1.0
CE2 A:TYR47 3.9 44.8 1.0
SD A:MET71 4.1 20.0 1.0
CE1 A:TYR47 4.2 46.2 1.0
CD2 A:TYR47 4.5 38.6 1.0
CG A:HIS51 4.8 15.3 1.0
CD1 A:TYR47 4.8 39.6 1.0
CG A:TYR47 5.0 31.8 1.0
CG1 A:ILE44 5.0 11.1 1.0
NE2 A:HIS51 5.0 13.4 1.0

Reference:

H.Riegler, T.Herter, I.Grishkovskaya, A.Lude, M.Ryngajllo, M.E.Bolger, B.Essigmann, B.Usadel. Crystal Structure and Functional Characterization of A Glucosamine-6-Phosphate N-Acetyltransferase From Arabidopsis Thaliana. Biochem.J. V. 443 427 2012.
ISSN: ISSN 0264-6021
PubMed: 22329777
DOI: 10.1042/BJ20112071
Page generated: Tue Dec 15 06:25:58 2020

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