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Sodium in PDB 3i78: 35/99/170/186/220-Loops of Fxa in Sgt

Enzymatic activity of 35/99/170/186/220-Loops of Fxa in Sgt

All present enzymatic activity of 35/99/170/186/220-Loops of Fxa in Sgt:
3.4.21.4;

Protein crystallography data

The structure of 35/99/170/186/220-Loops of Fxa in Sgt, PDB code: 3i78 was solved by M.J.Page, E.Di Cera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.94 / 3.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 113.710, 113.710, 52.616, 90.00, 90.00, 120.00
R / Rfree (%) 20.8 / 27.5

Sodium Binding Sites:

The binding sites of Sodium atom in the 35/99/170/186/220-Loops of Fxa in Sgt (pdb code 3i78). 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 35/99/170/186/220-Loops of Fxa in Sgt, PDB code: 3i78:

Sodium binding site 1 out of 1 in 3i78

Go back to Sodium Binding Sites List in 3i78
Sodium binding site 1 out of 1 in the 35/99/170/186/220-Loops of Fxa in Sgt


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of 35/99/170/186/220-Loops of Fxa in Sgt within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na301

b:52.4
occ:1.00
O A:ASP185A 2.6 59.9 1.0
O A:TYR185 2.7 56.4 1.0
O A:ARG222 2.8 58.4 1.0
C A:ASP185A 3.1 59.7 1.0
O A:LYS224 3.4 49.7 1.0
C A:TYR185 3.5 56.1 1.0
O A:LYS186 3.6 61.9 1.0
N A:THR185B 3.6 60.2 1.0
O A:ALA221 3.7 57.6 1.0
C A:ARG222 3.7 58.5 1.0
C A:ALA221 3.8 57.4 1.0
CA A:THR185B 3.8 61.1 1.0
C A:THR185B 3.8 61.4 1.0
O A:THR185B 4.0 61.5 1.0
CA A:ASP185A 4.1 59.1 1.0
N A:ASP185A 4.1 57.7 1.0
N A:ARG222 4.2 57.9 1.0
CA A:ALA221 4.2 57.2 1.0
N A:LYS186 4.3 61.7 1.0
CA A:TYR185 4.4 54.8 1.0
CB A:TYR185 4.4 54.2 1.0
N A:LYS223 4.4 58.6 1.0
CA A:ARG222 4.5 58.5 1.0
C A:LYS186 4.6 62.0 1.0
C A:LYS224 4.6 49.8 1.0
N A:TYR185 4.6 53.8 1.0
N A:LYS224 4.8 51.9 1.0
N A:GLY223A 4.8 56.2 1.0
CB A:ALA221 4.8 57.2 1.0
CA A:LYS223 4.9 58.2 1.0

Reference:

M.J.Page, E.Di Cera. Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold. J.Mol.Biol. V. 399 306 2010.
ISSN: ISSN 0022-2836
PubMed: 20399789
DOI: 10.1016/J.JMB.2010.04.024
Page generated: Mon Oct 7 10:42:27 2024

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