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Chlorine in PDB 3t4p: Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani in Complex with Designed Tetrapeptide

Enzymatic activity of Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani in Complex with Designed Tetrapeptide

All present enzymatic activity of Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani in Complex with Designed Tetrapeptide:
2.5.1.47;

Protein crystallography data

The structure of Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani in Complex with Designed Tetrapeptide, PDB code: 3t4p 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) 34.69 / 1.77
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 115.300, 61.930, 43.440, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani in Complex with Designed Tetrapeptide (pdb code 3t4p). 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 in Complex with Designed Tetrapeptide, PDB code: 3t4p:

Chlorine binding site 1 out of 1 in 3t4p

Go back to Chlorine Binding Sites List in 3t4p
Chlorine binding site 1 out of 1 in the Crystal Structure of O-Acetyl Serine Sulfhydrylase From Leishmania Donovani in Complex with Designed Tetrapeptide


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 in Complex with Designed Tetrapeptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:13.5
occ:1.00
 OG A:SER302 2.9 19.0 1.0
N A:GLY272 3.2 13.9 1.0
N A:GLY275 3.2 12.1 1.0
N A:SER302 3.3 12.2 1.0
CA A:GLY272 3.4 15.5 1.0
O A:SER302 3.5 12.1 1.0
C A:GLY272 3.6 16.8 1.0
O A:HOH516 3.7 19.2 1.0
CD A:PRO301 3.7 10.0 1.0
O A:GLY272 3.8 14.6 1.0
N A:SER274 3.9 16.0 1.0
CB A:SER302 3.9 13.6 1.0
CA A:GLY275 3.9 10.1 1.0
CA A:SER302 4.0 12.5 1.0
C2' A:LLP51 4.0 15.6 1.0
C A:SER274 4.1 12.7 1.0
CB A:PRO301 4.1 12.5 1.0
OG A:SER274 4.1 27.3 1.0
N A:PRO301 4.1 10.1 1.0
C A:SER302 4.1 11.3 1.0
CB A:CYS271 4.2 11.2 1.0
CB A:SER274 4.2 18.2 1.0
CA A:SER274 4.2 15.3 1.0
C A:PRO301 4.2 12.7 1.0
N A:PHE273 4.3 16.4 1.0
C A:CYS271 4.3 12.8 1.0
CA A:PRO301 4.4 10.9 1.0
CG A:PRO301 4.4 11.6 1.0
OH A:TYR307 4.5 21.7 1.0
CA A:CYS271 4.7 11.6 1.0
C A:PHE273 4.7 15.3 1.0
CE2 A:TYR307 4.8 17.2 1.0
CZ A:TYR307 4.8 20.3 1.0
N1 A:LLP51 4.8 15.8 1.0
SG A:CYS271 4.8 14.8 1.0
C2 A:LLP51 4.9 15.4 1.0
C A:ILE300 4.9 10.5 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 05:00:00 2024

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