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Chlorine in PDB 2ah2: Trypanosoma Cruzi Trans-Sialidase in Complex with 2,3-Difluorosialic Acid (Covalent Intermediate)

Enzymatic activity of Trypanosoma Cruzi Trans-Sialidase in Complex with 2,3-Difluorosialic Acid (Covalent Intermediate)

All present enzymatic activity of Trypanosoma Cruzi Trans-Sialidase in Complex with 2,3-Difluorosialic Acid (Covalent Intermediate):
3.2.1.18;

Protein crystallography data

The structure of Trypanosoma Cruzi Trans-Sialidase in Complex with 2,3-Difluorosialic Acid (Covalent Intermediate), PDB code: 2ah2 was solved by M.F.Amaya, A.G.Watts, I.Damager, A.Wehenkel, T.Nguyen, A.Buschiazzo, G.Paris, A.C.Frasch, S.G.Withers, P.M.Alzari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.40 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.149, 128.690, 54.298, 90.00, 108.74, 90.00
R / Rfree (%) 9.9 / 15.2

Other elements in 2ah2:

The structure of Trypanosoma Cruzi Trans-Sialidase in Complex with 2,3-Difluorosialic Acid (Covalent Intermediate) also contains other interesting chemical elements:

Fluorine (F) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Trypanosoma Cruzi Trans-Sialidase in Complex with 2,3-Difluorosialic Acid (Covalent Intermediate) (pdb code 2ah2). 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 Trypanosoma Cruzi Trans-Sialidase in Complex with 2,3-Difluorosialic Acid (Covalent Intermediate), PDB code: 2ah2:

Chlorine binding site 1 out of 1 in 2ah2

Go back to Chlorine Binding Sites List in 2ah2
Chlorine binding site 1 out of 1 in the Trypanosoma Cruzi Trans-Sialidase in Complex with 2,3-Difluorosialic Acid (Covalent Intermediate)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Trypanosoma Cruzi Trans-Sialidase in Complex with 2,3-Difluorosialic Acid (Covalent Intermediate) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1001

b:23.1
occ:1.00
 O A:HOH2289 2.9 36.4 1.0
O A:HOH2251 3.1 31.1 1.0
N A:HIS171 3.2 18.0 1.0
N A:LYS199 3.5 15.9 1.0
O A:HIS171 3.6 17.0 1.0
CB A:MET170 3.7 18.4 0.6
CB A:ASN198 3.7 13.6 1.0
CA A:MET170 3.8 19.3 0.6
CG A:ASN198 3.8 14.1 1.0
N A:LYS200 3.8 16.5 1.0
CG A:LYS200 3.9 23.1 1.0
CA A:MET170 3.9 20.6 0.5
CB A:LYS199 4.0 18.8 1.0
C A:MET170 4.0 18.5 0.6
CB A:MET170 4.0 20.0 0.5
CA A:HIS171 4.1 17.4 1.0
CB A:HIS171 4.1 18.9 1.0
C A:MET170 4.1 19.0 0.5
CA A:LYS199 4.1 17.2 1.0
CD A:LYS200 4.1 28.5 1.0
ND2 A:ASN198 4.1 15.2 1.0
OD1 A:ASN198 4.2 15.3 1.0
C A:HIS171 4.2 16.4 1.0
CE A:LYS200 4.3 34.0 1.0
C A:LYS199 4.3 17.7 1.0
C A:ASN198 4.4 14.6 1.0
CB A:LYS200 4.4 18.4 1.0
CA A:ASN198 4.6 14.3 1.0
CD2 A:HIS171 4.6 26.8 1.0
CG A:HIS171 4.7 21.4 1.0
CG A:LYS199 4.7 19.7 1.0
CA A:LYS200 4.8 17.3 1.0
CG A:MET170 4.8 21.2 0.5
O A:GLY169 4.9 25.2 1.0
CG A:MET170 5.0 17.1 0.6

Reference:

M.F.Amaya, A.G.Watts, I.Damager, A.Wehenkel, T.Nguyen, A.Buschiazzo, G.Paris, A.C.Frasch, S.G.Withers, P.M.Alzari. Structural Insights Into the Catalytic Mechanism of Trypanosoma Cruzi Trans-Sialidase Structure V. 12 775 2004.
ISSN: ISSN 0969-2126
PubMed: 15130470
DOI: 10.1016/J.STR.2004.02.036
Page generated: Sat Jul 20 05:14:17 2024

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