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Chlorine in PDB 4lgl: Crystal Structure of Glycine Decarboxylase P-Protein From Synechocystis Sp. Pcc 6803, Apo Form

Enzymatic activity of Crystal Structure of Glycine Decarboxylase P-Protein From Synechocystis Sp. Pcc 6803, Apo Form

All present enzymatic activity of Crystal Structure of Glycine Decarboxylase P-Protein From Synechocystis Sp. Pcc 6803, Apo Form:
1.4.4.2;

Protein crystallography data

The structure of Crystal Structure of Glycine Decarboxylase P-Protein From Synechocystis Sp. Pcc 6803, Apo Form, PDB code: 4lgl was solved by D.Hasse, E.Andersson, G.Carlsson, A.Masloboy, M.Hagemann, H.Bauwe, I.Andersson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 54.11 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 96.299, 135.814, 179.080, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 19.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Glycine Decarboxylase P-Protein From Synechocystis Sp. Pcc 6803, Apo Form (pdb code 4lgl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Glycine Decarboxylase P-Protein From Synechocystis Sp. Pcc 6803, Apo Form, PDB code: 4lgl:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 4lgl

Go back to Chlorine Binding Sites List in 4lgl
Chlorine binding site 1 out of 2 in the Crystal Structure of Glycine Decarboxylase P-Protein From Synechocystis Sp. Pcc 6803, Apo Form


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 Glycine Decarboxylase P-Protein From Synechocystis Sp. Pcc 6803, Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1002

b:48.7
occ:0.94
N A:SER80 3.4 36.0 1.0
CD A:PRO796 3.5 39.4 1.0
N A:GLN797 3.6 46.4 1.0
OG A:SER80 3.7 49.6 1.0
NE2 A:GLN797 3.7 82.8 1.0
CG A:GLN797 3.8 66.6 1.0
CB A:SER80 3.8 46.5 1.0
CB A:GLN797 3.8 57.4 1.0
N A:PRO796 3.8 36.1 1.0
CA A:GLY795 3.8 33.6 1.0
O A:MET794 4.0 47.0 1.0
CD A:GLN797 4.0 80.1 1.0
C A:GLY795 4.0 39.1 1.0
CA A:ALA79 4.2 44.2 1.0
CA A:SER80 4.2 38.1 1.0
C A:ALA79 4.3 42.7 1.0
CA A:GLN797 4.3 50.3 1.0
CG A:PRO796 4.4 48.4 1.0
N A:GLY798 4.6 38.7 1.0
C A:PRO796 4.6 46.1 1.0
O A:HOH1426 4.6 40.0 1.0
CA A:PRO796 4.6 44.6 1.0
CB A:PRO796 4.7 47.5 1.0
CB A:ALA79 4.7 43.5 1.0
N A:GLY795 4.8 37.0 1.0
C A:MET794 4.8 41.4 1.0
OE1 A:GLN797 4.9 85.0 1.0
O A:GLY795 4.9 41.0 1.0

Chlorine binding site 2 out of 2 in 4lgl

Go back to Chlorine Binding Sites List in 4lgl
Chlorine binding site 2 out of 2 in the Crystal Structure of Glycine Decarboxylase P-Protein From Synechocystis Sp. Pcc 6803, Apo Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Glycine Decarboxylase P-Protein From Synechocystis Sp. Pcc 6803, Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1002

b:33.7
occ:0.84
O B:HOH1313 3.1 39.6 1.0
O B:HOH1486 3.4 54.7 1.0
CD B:PRO796 3.4 25.2 1.0
N B:SER80 3.4 29.0 1.0
N B:GLN797 3.6 26.5 1.0
CB B:GLN797 3.7 37.6 1.0
CA B:GLY795 3.7 26.6 1.0
N B:PRO796 3.7 26.2 1.0
CG B:PRO796 3.8 31.9 1.0
CG B:GLN797 3.9 45.3 1.0
C B:GLY795 3.9 26.2 1.0
CB B:SER80 4.0 32.1 1.0
OG B:SER80 4.0 35.7 1.0
O B:MET794 4.0 28.4 1.0
CA B:ALA79 4.1 31.6 1.0
CD B:GLN797 4.1 59.3 1.0
NE2 B:GLN797 4.1 61.8 1.0
CA B:GLN797 4.2 27.2 1.0
C B:ALA79 4.3 31.6 1.0
CA B:SER80 4.3 34.0 1.0
O B:HOH1430 4.5 34.9 1.0
C B:PRO796 4.5 30.9 1.0
N B:GLY798 4.6 23.6 1.0
CA B:PRO796 4.6 27.2 1.0
N B:GLY795 4.7 26.8 1.0
CB B:ALA79 4.7 34.9 1.0
OE1 B:GLN797 4.8 58.5 1.0
C B:MET794 4.8 25.5 1.0
O B:GLY795 4.8 25.9 1.0
CB B:PRO796 4.9 27.6 1.0
C B:GLN797 5.0 29.3 1.0
O B:PRO78 5.0 28.2 1.0

Reference:

D.Hasse, E.Andersson, G.Carlsson, A.Masloboy, M.Hagemann, H.Bauwe, I.Andersson. Structure of the Homodimeric Glycine Decarboxylase P-Protein From Synechocystis Sp. Pcc 6803 Suggests A Mechanism For Redox Regulation. J.Biol.Chem. V. 288 35333 2013.
ISSN: ISSN 0021-9258
PubMed: 24121504
DOI: 10.1074/JBC.M113.509976
Page generated: Sat Dec 12 10:52:47 2020

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