Atomistry » Sodium » PDB 4nxz-4obo » 4o0g
Atomistry »
  Sodium »
    PDB 4nxz-4obo »
      4o0g »

Sodium in PDB 4o0g: Crystal Structure of the Human L-Asparaginase Protein T219V Mutant

Enzymatic activity of Crystal Structure of the Human L-Asparaginase Protein T219V Mutant

All present enzymatic activity of Crystal Structure of the Human L-Asparaginase Protein T219V Mutant:
3.4.19.5; 3.5.1.1;

Protein crystallography data

The structure of Crystal Structure of the Human L-Asparaginase Protein T219V Mutant, PDB code: 4o0g was solved by J.Nomme, A.Lavie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.18 / 2.10
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 59.439, 59.439, 306.794, 90.00, 90.00, 120.00
R / Rfree (%) 16.5 / 23.6

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Human L-Asparaginase Protein T219V Mutant (pdb code 4o0g). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of the Human L-Asparaginase Protein T219V Mutant, PDB code: 4o0g:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 4o0g

Go back to Sodium Binding Sites List in 4o0g
Sodium binding site 1 out of 2 in the Crystal Structure of the Human L-Asparaginase Protein T219V Mutant


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 the Human L-Asparaginase Protein T219V Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na401

b:31.1
occ:1.00
O A:CYS65 2.1 33.5 1.0
O A:ALA63 2.3 27.7 1.0
O A:GLU56 2.4 28.8 1.0
O A:ASP58 2.6 41.6 1.0
O A:PHE61 2.7 30.8 1.0
O A:LEU55 2.9 23.4 1.0
C A:CYS65 3.2 28.1 1.0
C A:GLU56 3.2 28.0 1.0
C A:ASP58 3.5 37.9 1.0
C A:ALA63 3.5 25.4 1.0
CA A:GLU56 3.6 21.9 1.0
N A:CYS65 3.6 29.5 1.0
C A:PHE61 3.7 28.9 1.0
CA A:CYS65 3.9 31.4 1.0
C A:GLY64 3.9 29.6 1.0
C A:LEU55 4.0 20.8 1.0
CA A:PRO59 4.0 37.1 1.0
N A:ALA63 4.0 25.6 1.0
N A:ASP58 4.1 32.6 1.0
N A:PRO59 4.1 37.9 1.0
N A:GLY66 4.2 29.6 1.0
N A:PHE61 4.2 30.9 1.0
CA A:PHE61 4.2 30.4 1.0
N A:ASP57 4.3 29.2 1.0
N A:GLU56 4.3 18.6 1.0
CB A:PHE61 4.3 29.6 1.0
O A:GLY64 4.3 37.3 1.0
C A:PRO59 4.3 38.0 1.0
CA A:ALA63 4.4 24.3 1.0
N A:GLY64 4.4 28.7 1.0
CA A:GLY66 4.4 29.2 1.0
CB A:CYS65 4.4 30.9 1.0
C A:ASP57 4.4 30.6 1.0
CA A:ASP58 4.4 33.9 1.0
CA A:GLY64 4.4 29.2 1.0
O A:PRO59 4.6 36.0 1.0
C A:GLY66 4.6 28.8 1.0
N A:ASN62 4.7 26.8 1.0
CA A:ASP57 4.8 31.0 1.0
CB A:GLU56 4.8 22.2 1.0
N A:SER67 4.9 28.0 1.0
O A:ASP57 4.9 31.5 1.0
N A:GLU60 4.9 34.9 1.0
CB A:ALA63 4.9 23.5 1.0

Sodium binding site 2 out of 2 in 4o0g

Go back to Sodium Binding Sites List in 4o0g
Sodium binding site 2 out of 2 in the Crystal Structure of the Human L-Asparaginase Protein T219V Mutant


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 the Human L-Asparaginase Protein T219V Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na401

b:24.8
occ:1.00
O B:CYS65 2.4 32.0 1.0
O B:ASP58 2.4 30.3 1.0
O B:ALA63 2.4 25.5 1.0
O B:LEU55 2.5 22.4 1.0
O B:GLU56 2.7 25.2 1.0
O B:PHE61 2.9 33.0 1.0
C B:GLU56 3.1 25.6 1.0
C B:ASP58 3.3 27.6 1.0
C B:CYS65 3.5 26.9 1.0
CA B:GLU56 3.5 23.0 1.0
N B:ASP58 3.5 26.7 1.0
C B:LEU55 3.6 23.0 1.0
C B:ALA63 3.6 24.3 1.0
C B:PHE61 3.7 29.2 1.0
CB B:PHE61 3.8 28.6 1.0
N B:CYS65 3.8 26.0 1.0
N B:ASP57 3.9 25.1 1.0
CA B:ASP58 3.9 26.3 1.0
N B:PHE61 4.0 30.4 1.0
CA B:PHE61 4.0 29.6 1.0
N B:GLU56 4.0 21.3 1.0
C B:ASP57 4.1 25.8 1.0
N B:PRO59 4.2 25.7 1.0
CA B:CYS65 4.2 28.0 1.0
C B:GLY64 4.4 26.8 1.0
N B:ALA63 4.4 24.3 1.0
CB B:ALA63 4.4 23.6 1.0
CA B:ALA63 4.5 24.0 1.0
N B:GLY66 4.5 26.8 1.0
CA B:PRO59 4.5 26.2 1.0
CA B:ASP57 4.5 25.2 1.0
CB B:ASP58 4.6 28.3 1.0
N B:GLY64 4.6 26.1 1.0
CB B:CYS65 4.7 26.6 1.0
CA B:GLY66 4.7 24.9 1.0
CA B:GLY64 4.7 26.6 1.0
O B:ASP57 4.8 24.4 1.0
C B:PRO59 4.8 28.3 1.0
CA B:LEU55 4.8 24.6 1.0
CB B:GLU56 4.9 22.4 1.0
N B:ASN62 4.9 25.1 1.0
CG B:PHE61 5.0 29.3 1.0

Reference:

J.Nomme, Y.Su, A.Lavie. Elucidation of the Specific Function of the Conserved Threonine Triad Responsible For Human L-Asparaginase Autocleavage and Substrate Hydrolysis. J.Mol.Biol. V. 426 2471 2014.
ISSN: ISSN 0022-2836
PubMed: 24768817
DOI: 10.1016/J.JMB.2014.04.016
Page generated: Mon Oct 7 17:21:11 2024

Last articles

Cl in 5SYI
Cl in 5SYH
Cl in 5SXX
Cl in 5SXT
Cl in 5SXU
Cl in 5SXS
Cl in 5SXR
Cl in 5SXQ
Cl in 5SX3
Cl in 5SWR
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy