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Chlorine in PDB 2q3b: 1.8 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (Oass) Holoenzyme From Mycobacterium Tuberculosis

Enzymatic activity of 1.8 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (Oass) Holoenzyme From Mycobacterium Tuberculosis

All present enzymatic activity of 1.8 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (Oass) Holoenzyme From Mycobacterium Tuberculosis:
2.5.1.47;

Protein crystallography data

The structure of 1.8 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (Oass) Holoenzyme From Mycobacterium Tuberculosis, PDB code: 2q3b was solved by G.Schneider, R.Schnell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.96 / 1.80
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 70.991, 70.991, 179.624, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 19.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the 1.8 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (Oass) Holoenzyme From Mycobacterium Tuberculosis (pdb code 2q3b). 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 1.8 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (Oass) Holoenzyme From Mycobacterium Tuberculosis, PDB code: 2q3b:

Chlorine binding site 1 out of 1 in 2q3b

Go back to Chlorine Binding Sites List in 2q3b
Chlorine binding site 1 out of 1 in the 1.8 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (Oass) Holoenzyme From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 1.8 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (Oass) Holoenzyme From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl400

b:28.4
occ:1.00
 OG1 A:THR71 3.0 26.5 1.0
O A:HOH566 3.1 37.8 1.0
N A:GLY73 3.3 23.2 1.0
NE2 A:GLN144 3.4 22.4 1.0
CA A:GLY73 3.5 22.3 1.0
C A:GLY73 3.6 21.3 1.0
N A:THR75 3.6 18.2 1.0
C1 A:MPD404 3.6 58.2 1.0
CB A:THR75 3.6 18.4 1.0
CM A:MPD404 3.7 58.6 1.0
OG1 A:THR75 3.9 17.9 1.0
N A:ASN74 3.9 20.0 1.0
CB A:THR71 3.9 25.0 1.0
O A:GLY73 3.9 21.4 1.0
N A:SER72 4.1 24.8 1.0
C2 A:MPD404 4.2 58.5 1.0
CA A:THR75 4.2 17.8 1.0
CD A:GLN144 4.3 21.2 1.0
CA A:THR71 4.3 23.9 1.0
OE1 A:GLN144 4.3 21.2 1.0
C A:SER72 4.4 24.6 1.0
N A:GLY76 4.4 16.8 1.0
C3 A:MPD404 4.6 58.7 1.0
C A:THR71 4.6 24.5 1.0
C A:ASN74 4.7 18.2 1.0
O A:HOH443 4.7 20.5 1.0
C A:THR75 4.8 17.4 1.0
CA A:ASN74 4.8 19.2 1.0
CG2 A:THR75 4.9 19.0 1.0
CA A:SER72 4.9 25.0 1.0

Reference:

R.Schnell, W.Oehlmann, M.Singh, G.Schneider. Structural Insights Into Catalysis and Inhibition of O-Acetylserine Sulfhydrylase From Mycobacterium Tuberculosis: Crystal Structures of the Enzyme {Alpha}-Aminoacrylate Intermediate and An Enzyme-Inhibitor Complex. J.Biol.Chem. V. 282 23473 2007.
ISSN: ISSN 0021-9258
PubMed: 17567578
DOI: 10.1074/JBC.M703518200
Page generated: Sat Jul 20 10:25:18 2024

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