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Sodium in PDB 3spx: Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani

Enzymatic activity of Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani

All present enzymatic activity of Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani:
2.5.1.47;

Protein crystallography data

The structure of Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani, PDB code: 3spx was solved by I.Raj, S.Gourinath, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.20 / 1.79
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 115.266, 61.974, 43.427, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 21.6

Other elements in 3spx:

The structure of Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani (pdb code 3spx). 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 O-Acetyl Serine Sulfhydrylase From Leishmania Donovani, PDB code: 3spx:

Sodium binding site 1 out of 1 in 3spx

Go back to Sodium Binding Sites List in 3spx
Sodium binding site 1 out of 1 in the Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani


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 O-Acetyl Serine Sulfhydrylase From Leishmania Donovani within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na336

b:24.9
occ:1.00
 OE1 A:GLU44 2.9 16.4 1.0
OE2 A:GLU44 3.0 14.1 1.0
O A:HOH504 3.2 40.5 1.0
CD A:GLU44 3.3 18.0 1.0
O A:HOH503 3.5 52.3 1.0
O A:HOH502 3.5 15.3 0.5
CE1 A:PHE303 4.0 16.4 1.0
CD1 A:PHE303 4.2 13.7 1.0
O A:CYS43 4.2 10.9 1.0
CZ A:PHE303 4.3 13.4 1.0
CG A:PHE303 4.6 13.2 1.0
CA A:GLU44 4.6 13.0 1.0
CE2 A:PHE303 4.7 15.4 1.0
CG A:GLU44 4.7 12.7 1.0
CD2 A:PHE303 4.8 14.9 1.0
C A:CYS43 5.0 11.9 1.0
CB A:GLU44 5.0 9.2 1.0

Reference:

I.Raj, S.Kumar, S.Gourinath. The Narrow Active-Site Cleft of O-Acetylserine Sulfhydrylase From Leishmania Donovani Allows Complex Formation with Serine Acetyltransferases with A Range of C-Terminal Sequences Acta Crystallogr.,Sect.D V. 68 909 2012.
ISSN: ISSN 0907-4449
PubMed: 22868756
DOI: 10.1107/S0907444912016459
Page generated: Mon Oct 7 12:59:39 2024

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