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Chlorine 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:

Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani, PDB code: 3spx:

Chlorine binding site 1 out of 1 in 3spx

Go back to Chlorine Binding Sites List in 3spx
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl335

b:11.4
occ:1.00
 OG A:SER302 2.9 15.7 1.0
N A:GLY272 3.2 14.2 1.0
N A:GLY275 3.2 12.3 1.0
OG A:SER274 3.4 24.0 1.0
N A:SER302 3.4 12.1 1.0
CA A:GLY272 3.5 13.2 1.0
O A:SER302 3.5 12.3 1.0
C A:GLY272 3.6 14.5 1.0
CD A:PRO301 3.7 10.2 1.0
O A:GLY272 3.8 14.1 1.0
O A:HOH527 3.8 16.8 1.0
CB A:SER302 3.9 12.3 1.0
N A:SER274 3.9 16.8 1.0
CA A:GLY275 4.0 11.8 1.0
CA A:SER302 4.0 10.7 1.0
C2' A:LLP51 4.0 12.6 1.0
N A:PRO301 4.0 11.5 1.0
CB A:PRO301 4.1 12.6 1.0
C A:SER274 4.1 13.2 1.0
C A:SER302 4.1 10.5 1.0
CB A:CYS271 4.1 10.9 1.0
CA A:SER274 4.2 16.5 1.0
C A:PRO301 4.2 11.6 1.0
N A:PHE273 4.3 14.8 1.0
OH A:TYR307 4.3 18.0 1.0
CA A:PRO301 4.3 10.8 1.0
CG A:PRO301 4.3 12.2 1.0
C A:CYS271 4.4 11.9 1.0
CB A:SER274 4.4 17.9 1.0
C A:PHE273 4.7 15.7 1.0
CA A:CYS271 4.7 10.9 1.0
CZ A:TYR307 4.7 16.5 1.0
SG A:CYS271 4.8 13.8 1.0
N1 A:LLP51 4.8 13.1 1.0
CE2 A:TYR307 4.8 16.1 1.0
C A:ILE300 4.9 11.2 1.0
C2 A:LLP51 5.0 14.8 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: Sun Jul 21 04:43:21 2024

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