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Sodium in PDB 1za2: Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution

Enzymatic activity of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution

All present enzymatic activity of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution:
2.1.3.2;

Protein crystallography data

The structure of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution, PDB code: 1za2 was solved by J.Wang, K.A.Stieglitz, J.P.Cardia, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.50
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 121.442, 121.442, 142.547, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 25.1

Other elements in 1za2:

The structure of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution (pdb code 1za2). 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 Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution, PDB code: 1za2:

Sodium binding site 1 out of 1 in 1za2

Go back to Sodium Binding Sites List in 1za2
Sodium binding site 1 out of 1 in the Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in the Presence of Ctp, Carbamoyl Phosphate at 2.50 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na311

b:40.6
occ:1.00
O A:HOH379 2.2 70.3 1.0
O A:HOH323 3.0 39.3 1.0
O A:HOH450 3.3 94.2 1.0
OG A:SER69 4.0 39.7 1.0
CE1 A:HIS64 4.4 29.1 1.0
O A:HOH391 4.5 69.0 1.0
ND1 A:HIS64 4.5 30.1 1.0
CB A:SER69 4.7 31.0 1.0
CA A:SER69 4.7 30.9 1.0

Reference:

J.Wang, K.A.Stieglitz, J.P.Cardia, E.R.Kantrowitz. Structural Basis For Ordered Substrate Binding and Cooperativity in Aspartate Transcarbamoylase Proc.Natl.Acad.Sci.Usa V. 102 8881 2005.
ISSN: ISSN 0027-8424
PubMed: 15951418
DOI: 10.1073/PNAS.0503742102
Page generated: Tue Dec 15 05:44:22 2020

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