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Sodium in PDB 4y23: Crystal Structure of T399A Precursor Mutant Protein of Gamma-Glutamyl Transpeptidase From Bacillus Licheniformis

Enzymatic activity of Crystal Structure of T399A Precursor Mutant Protein of Gamma-Glutamyl Transpeptidase From Bacillus Licheniformis

All present enzymatic activity of Crystal Structure of T399A Precursor Mutant Protein of Gamma-Glutamyl Transpeptidase From Bacillus Licheniformis:
2.3.2.2;

Protein crystallography data

The structure of Crystal Structure of T399A Precursor Mutant Protein of Gamma-Glutamyl Transpeptidase From Bacillus Licheniformis, PDB code: 4y23 was solved by A.Pica, A.Merlino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.56 / 2.89
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 59.438, 59.438, 281.930, 90.00, 90.00, 120.00
R / Rfree (%) 22.1 / 27.6

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of T399A Precursor Mutant Protein of Gamma-Glutamyl Transpeptidase From Bacillus Licheniformis (pdb code 4y23). 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 T399A Precursor Mutant Protein of Gamma-Glutamyl Transpeptidase From Bacillus Licheniformis, PDB code: 4y23:

Sodium binding site 1 out of 1 in 4y23

Go back to Sodium Binding Sites List in 4y23
Sodium binding site 1 out of 1 in the Crystal Structure of T399A Precursor Mutant Protein of Gamma-Glutamyl Transpeptidase From Bacillus Licheniformis


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 T399A Precursor Mutant Protein of Gamma-Glutamyl Transpeptidase From Bacillus Licheniformis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na601

b:44.2
occ:1.00
 O A:HOH706 2.4 40.1 1.0
O A:HOH710 2.5 52.9 1.0
OE1 A:GLU419 2.9 69.1 1.0
OD2 A:ASP441 3.2 55.1 1.0
OE2 A:GLU438 3.5 47.5 1.0
OD1 A:ASP441 3.9 45.5 1.0
CD A:GLU419 3.9 65.2 1.0
CG A:ASP441 3.9 50.9 1.0
OE2 A:GLU419 4.3 70.2 1.0
NH1 A:ARG109 4.4 50.0 1.0
OG A:SER460 4.4 43.9 1.0
O A:GLU419 4.5 64.0 1.0
CA A:GLY482 4.6 48.1 1.0
CD A:GLU438 4.7 51.7 1.0
NH2 A:ARG109 4.7 45.8 1.0
CA A:GLU419 4.7 52.4 1.0
OG1 A:THR417 4.9 48.3 1.0
CG2 A:THR417 5.0 47.8 1.0
N A:SER461 5.0 44.5 1.0

Reference:

A.Pica, M.C.Chi, Y.Y.Chen, M.D'ischia, L.L.Lin, A.Merlino. The Maturation Mechanism of Gamma-Glutamyl Transpeptidases: Insights From the Crystal Structure of A Precursor Mimic of the Enzyme From Bacillus Licheniformis and From Site-Directed Mutagenesis Studies. Biochim.Biophys.Acta V.1864 195 2015.
ISSN: ISSN 0006-3002
PubMed: 26536828
DOI: 10.1016/J.BBAPAP.2015.10.006
Page generated: Sun Aug 17 22:33:48 2025

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