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Sodium in PDB 1y7w: Crystal Structure of A Halotolerant Carbonic Anhydrase From Dunaliella Salina

Enzymatic activity of Crystal Structure of A Halotolerant Carbonic Anhydrase From Dunaliella Salina

All present enzymatic activity of Crystal Structure of A Halotolerant Carbonic Anhydrase From Dunaliella Salina:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of A Halotolerant Carbonic Anhydrase From Dunaliella Salina, PDB code: 1y7w was solved by L.Premkumar, H.M.Greenblatt, U.K.Bageshwar, T.Savchenko, I.Gokhman, J.L.Sussman, A.Zamir, Israel Structural Proteomics Center (Ispc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.95 / 1.86
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.022, 119.835, 58.442, 90.00, 94.55, 90.00
R / Rfree (%) 16.7 / 20.2

Other elements in 1y7w:

The structure of Crystal Structure of A Halotolerant Carbonic Anhydrase From Dunaliella Salina also contains other interesting chemical elements:

Zinc (Zn) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of A Halotolerant Carbonic Anhydrase From Dunaliella Salina (pdb code 1y7w). 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 A Halotolerant Carbonic Anhydrase From Dunaliella Salina, PDB code: 1y7w:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 1y7w

Go back to Sodium Binding Sites List in 1y7w
Sodium binding site 1 out of 2 in the Crystal Structure of A Halotolerant Carbonic Anhydrase From Dunaliella Salina


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 A Halotolerant Carbonic Anhydrase From Dunaliella Salina within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na281

b:23.2
occ:1.00
O A:HOH343 2.2 30.0 1.0
O A:HOH379 2.3 35.5 1.0
O A:GLY67 2.3 22.8 1.0
O A:GLN69 2.4 24.2 1.0
O A:GLY72 2.4 22.8 1.0
C A:GLY67 3.4 21.0 1.0
C A:GLY72 3.4 22.5 1.0
C A:GLN69 3.6 27.0 1.0
N A:GLY72 3.9 24.3 1.0
CA A:GLY72 4.0 22.7 1.0
N A:GLN69 4.0 25.2 1.0
CA A:GLY67 4.1 20.1 1.0
O A:ALA70 4.2 27.4 1.0
C A:ALA68 4.2 24.5 1.0
OG1 A:THR74 4.2 19.8 1.0
N A:ALA68 4.3 21.4 1.0
O A:HOH338 4.4 26.9 1.0
C A:ALA70 4.4 25.9 1.0
CA A:GLN69 4.4 26.8 1.0
N A:ILE73 4.5 21.2 1.0
N A:ALA70 4.5 27.2 1.0
CA A:ALA70 4.6 26.4 1.0
CA A:ALA68 4.6 24.1 1.0
O A:HOH467 4.6 41.5 1.0
O A:ALA68 4.6 25.9 1.0
O A:ASP66 4.7 21.7 1.0
N A:THR74 4.8 20.4 1.0
CA A:ILE73 4.8 19.2 1.0
C A:ILE73 4.9 20.1 1.0

Sodium binding site 2 out of 2 in 1y7w

Go back to Sodium Binding Sites List in 1y7w
Sodium binding site 2 out of 2 in the Crystal Structure of A Halotolerant Carbonic Anhydrase From Dunaliella Salina


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 A Halotolerant Carbonic Anhydrase From Dunaliella Salina within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na282

b:19.7
occ:1.00
O B:GLY67 2.3 18.4 1.0
O B:GLN69 2.4 19.8 1.0
O B:HOH336 2.5 26.0 1.0
O B:HOH333 2.5 19.9 1.0
O B:HOH306 2.5 22.7 1.0
O B:GLY72 2.5 20.2 1.0
C B:GLY67 3.4 19.6 1.0
C B:GLY72 3.5 21.8 1.0
C B:GLN69 3.6 21.4 1.0
O B:HOH418 3.8 35.4 1.0
N B:GLY72 3.9 22.9 1.0
N B:GLN69 4.0 20.7 1.0
CA B:GLY72 4.1 21.2 1.0
CA B:GLY67 4.1 18.7 1.0
O B:ALA70 4.2 24.1 1.0
OG1 B:THR74 4.2 18.5 1.0
C B:ALA70 4.2 22.9 1.0
C B:ALA68 4.3 20.0 1.0
CA B:ALA70 4.4 22.4 1.0
N B:ALA68 4.4 19.1 1.0
O B:HOH365 4.4 24.2 1.0
N B:ALA70 4.4 21.2 1.0
CA B:GLN69 4.5 20.2 1.0
CA B:ALA68 4.6 18.5 1.0
N B:ILE73 4.6 20.9 1.0
O B:HOH450 4.6 45.8 1.0
N B:ASP71 4.7 24.4 1.0
O B:ASP66 4.8 20.0 1.0
CA B:ILE73 4.8 19.4 1.0
N B:THR74 4.9 19.9 1.0
O B:ALA68 4.9 19.4 1.0
C B:ASP71 5.0 24.6 1.0

Reference:

L.Premkumar, H.M.Greenblatt, U.K.Bageshwar, T.Savchenko, I.Gokhman, J.L.Sussman, A.Zamir. Three-Dimensional Structure of A Halotolerant Algal Carbonic Anhydrase Predicts Halotolerance of A Mammalian Homolog. Proc.Natl.Acad.Sci.Usa V. 102 7493 2005.
ISSN: ISSN 0027-8424
PubMed: 15894606
DOI: 10.1073/PNAS.0502829102
Page generated: Tue Dec 15 05:42:09 2020

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