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Chlorine in PDB 3hfs: Structure of Apo Anthocyanidin Reductase From Vitis Vinifera

Enzymatic activity of Structure of Apo Anthocyanidin Reductase From Vitis Vinifera

All present enzymatic activity of Structure of Apo Anthocyanidin Reductase From Vitis Vinifera:
1.3.1.77;

Protein crystallography data

The structure of Structure of Apo Anthocyanidin Reductase From Vitis Vinifera, PDB code: 3hfs was solved by M.Gargouri, C.Mauge, B.Langlois D'estaintot, T.Granier, C.Manigan, B.Gallois, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.31 / 3.17
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 84.518, 51.012, 86.113, 90.00, 110.31, 90.00
R / Rfree (%) 22.1 / 29.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Apo Anthocyanidin Reductase From Vitis Vinifera (pdb code 3hfs). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Apo Anthocyanidin Reductase From Vitis Vinifera, PDB code: 3hfs:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 3hfs

Go back to Chlorine Binding Sites List in 3hfs
Chlorine binding site 1 out of 2 in the Structure of Apo Anthocyanidin Reductase From Vitis Vinifera


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Apo Anthocyanidin Reductase From Vitis Vinifera within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl339

b:61.5
occ:1.00
N A:VAL21 2.8 41.8 1.0
N A:PHE20 3.3 43.3 1.0
CB A:PHE20 3.4 42.9 1.0
CB A:VAL21 3.5 41.2 1.0
CA A:PHE20 3.6 42.9 1.0
C A:PHE20 3.7 42.3 1.0
N A:VAL91 3.7 42.2 1.0
CA A:VAL21 3.7 41.4 1.0
CG2 A:VAL21 3.8 40.4 1.0
C A:GLY19 4.1 43.6 1.0
CA A:PRO90 4.1 41.0 1.0
CB A:VAL91 4.2 42.6 1.0
CD2 A:PHE20 4.2 43.6 1.0
CG A:PHE20 4.2 43.1 1.0
CA A:GLY19 4.4 43.9 1.0
C A:PRO90 4.4 41.6 1.0
CG1 A:VAL87 4.4 39.6 1.0
CB A:PRO90 4.5 41.0 1.0
CG2 A:VAL91 4.5 42.2 1.0
CA A:VAL91 4.5 42.7 1.0
O A:VAL91 4.5 43.9 1.0
N A:ALA22 4.5 41.3 1.0
C A:VAL21 4.7 41.4 1.0
O A:PHE20 4.9 42.1 1.0
CG1 A:VAL21 4.9 41.2 1.0
O A:GLY19 5.0 43.2 1.0

Chlorine binding site 2 out of 2 in 3hfs

Go back to Chlorine Binding Sites List in 3hfs
Chlorine binding site 2 out of 2 in the Structure of Apo Anthocyanidin Reductase From Vitis Vinifera


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Apo Anthocyanidin Reductase From Vitis Vinifera within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl339

b:53.9
occ:1.00
N B:VAL91 3.2 42.7 1.0
CA B:PRO90 3.5 41.0 1.0
CG2 B:VAL21 3.5 40.3 1.0
N B:VAL21 3.6 41.1 1.0
CG1 B:VAL87 3.8 39.6 1.0
C B:PRO90 3.8 41.7 1.0
N B:PHE20 3.9 43.0 1.0
CB B:VAL21 3.9 40.7 1.0
CB B:PRO90 4.0 41.0 1.0
CB B:VAL91 4.2 43.2 1.0
CA B:VAL91 4.2 43.6 1.0
CB B:PHE20 4.2 42.8 1.0
CA B:VAL21 4.3 40.8 1.0
O B:VAL91 4.3 45.2 1.0
CA B:PHE20 4.4 42.5 1.0
CA B:GLY19 4.5 43.3 1.0
C B:PHE20 4.5 41.9 1.0
C B:GLY19 4.5 43.2 1.0
CB B:VAL87 4.7 39.6 1.0
O B:THR89 4.7 40.2 1.0
N B:PRO90 4.7 40.5 1.0
C B:VAL91 4.8 45.1 1.0
N B:ALA22 4.8 40.8 1.0
CG2 B:VAL87 4.9 39.1 1.0
CG2 B:VAL91 5.0 43.0 1.0

Reference:

M.Gargouri, C.Manigand, C.Mauge, T.Granier, B.Langlois D'estaintot, O.Cala, I.Pianet, K.Bathany, J.Chaudiere, B.Gallois. Structure and Epimerase Activity of Anthocyanidin Reductase From Vitis Vinifera. Acta Crystallogr.,Sect.D V. 65 989 2009.
ISSN: ISSN 0907-4449
PubMed: 19690377
DOI: 10.1107/S0907444909025013
Page generated: Sat Dec 12 09:45:40 2020

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