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Chlorine in PDB 4fls: Crystal Structure of Amylosucrase Inactive Double Mutant F290K-E328Q From Neisseria Polysaccharea in Complex with Sucrose.

Enzymatic activity of Crystal Structure of Amylosucrase Inactive Double Mutant F290K-E328Q From Neisseria Polysaccharea in Complex with Sucrose.

All present enzymatic activity of Crystal Structure of Amylosucrase Inactive Double Mutant F290K-E328Q From Neisseria Polysaccharea in Complex with Sucrose.:
2.4.1.4;

Protein crystallography data

The structure of Crystal Structure of Amylosucrase Inactive Double Mutant F290K-E328Q From Neisseria Polysaccharea in Complex with Sucrose., PDB code: 4fls was solved by F.Guerin, E.Champion, C.Moulis, S.Barbe, T.H.Tran, S.Morel, K.Descroix, P.Monsan, L.A.Mulard, M.Remaud-Simeon, I.Andre, L.Mourey, S.Tranier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 11.98 / 2.30
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 95.110, 114.700, 54.620, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 22

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Amylosucrase Inactive Double Mutant F290K-E328Q From Neisseria Polysaccharea in Complex with Sucrose. (pdb code 4fls). 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 Amylosucrase Inactive Double Mutant F290K-E328Q From Neisseria Polysaccharea in Complex with Sucrose., PDB code: 4fls:

Chlorine binding site 1 out of 1 in 4fls

Go back to Chlorine Binding Sites List in 4fls
Chlorine binding site 1 out of 1 in the Crystal Structure of Amylosucrase Inactive Double Mutant F290K-E328Q From Neisseria Polysaccharea in Complex with Sucrose.


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 Amylosucrase Inactive Double Mutant F290K-E328Q From Neisseria Polysaccharea in Complex with Sucrose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl702

b:18.9
occ:1.00
 O1' A:SUC700 3.1 13.9 1.0
O A:HOH817 3.1 13.6 1.0
N A:ILE330 3.1 13.9 1.0
O A:HOH1080 3.1 16.8 1.0
O A:HOH1072 3.3 19.2 1.0
C1' A:SUC700 3.6 13.9 1.0
CA A:ILE330 3.9 14.0 1.0
O A:ILE330 4.0 14.0 1.0
CB A:ILE330 4.0 14.0 1.0
NZ A:LYS290 4.0 12.8 1.0
CA A:ALA329 4.0 14.0 1.0
C A:ALA329 4.1 13.9 1.0
C A:ILE330 4.1 14.0 1.0
CG1 A:VAL331 4.3 13.7 1.0
CG1 A:ILE330 4.4 14.0 1.0
C3' A:SUC700 4.4 14.1 1.0
O A:GLN328 4.4 15.2 1.0
O4' A:SUC700 4.6 14.3 1.0
C2' A:SUC700 4.6 14.0 1.0
NH2 A:ARG226 4.7 15.3 1.0
CB A:ALA289 4.8 12.4 1.0
N A:VAL331 4.9 14.0 1.0
N A:ALA329 4.9 14.2 1.0
CB A:ALA329 5.0 14.0 1.0

Reference:

E.Champion, F.Guerin, C.Moulis, S.Barbe, T.H.Tran, S.Morel, K.Descroix, P.Monsan, L.Mourey, L.A.Mulard, S.Tranier, M.Remaud-Simeon, I.Andre. Applying Pairwise Combinations of Amino Acid Mutations For Sorting Out Highly Efficient Glucosylation Tools For Chemo-Enzymatic Synthesis of Bacterial Oligosaccharides. J.Am.Chem.Soc. V. 134 18677 2012.
ISSN: ISSN 0002-7863
PubMed: 23072374
DOI: 10.1021/JA306845B
Page generated: Fri Jul 11 15:16:27 2025

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