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Chlorine in PDB 4guf: 1.5 Angstrom Crystal Structure of the Salmonella Enterica 3- Dehydroquinate Dehydratase (Arod) E86A Mutant

Enzymatic activity of 1.5 Angstrom Crystal Structure of the Salmonella Enterica 3- Dehydroquinate Dehydratase (Arod) E86A Mutant

All present enzymatic activity of 1.5 Angstrom Crystal Structure of the Salmonella Enterica 3- Dehydroquinate Dehydratase (Arod) E86A Mutant:
4.2.1.10;

Protein crystallography data

The structure of 1.5 Angstrom Crystal Structure of the Salmonella Enterica 3- Dehydroquinate Dehydratase (Arod) E86A Mutant, PDB code: 4guf was solved by S.H.Light, G.Minasov, M.-E.Duban, L.Shuvalova, K.Kwon, A.Lavie, W.F.Anderson, Center For Structural Genomics Of Infectious Diseases(Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.43 / 1.50
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 36.771, 45.552, 81.059, 93.90, 101.41, 105.90
R / Rfree (%) 16.7 / 19.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the 1.5 Angstrom Crystal Structure of the Salmonella Enterica 3- Dehydroquinate Dehydratase (Arod) E86A Mutant (pdb code 4guf). 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 1.5 Angstrom Crystal Structure of the Salmonella Enterica 3- Dehydroquinate Dehydratase (Arod) E86A Mutant, PDB code: 4guf:

Chlorine binding site 1 out of 1 in 4guf

Go back to Chlorine Binding Sites List in 4guf
Chlorine binding site 1 out of 1 in the 1.5 Angstrom Crystal Structure of the Salmonella Enterica 3- Dehydroquinate Dehydratase (Arod) E86A Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 1.5 Angstrom Crystal Structure of the Salmonella Enterica 3- Dehydroquinate Dehydratase (Arod) E86A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl301

b:19.1
occ:1.00
 O B:HOH419 3.1 19.4 1.0
N B:PHE118 3.3 14.5 1.0
ND2 B:ASN142 3.3 13.5 1.0
O B:HOH572 3.3 34.7 1.0
N B:LEU117 3.6 11.8 1.0
CD2 B:PHE118 3.7 20.2 1.0
CB B:GLU116 3.8 13.6 1.0
O B:SER141 3.8 10.9 1.0
CB B:PHE118 3.9 17.6 1.0
CB B:LEU117 4.0 12.9 1.0
CA B:LEU117 4.1 12.8 1.0
C B:GLU116 4.1 12.4 1.0
CA B:PHE118 4.1 16.5 1.0
C B:LEU117 4.1 13.8 1.0
CG B:PHE118 4.2 19.5 1.0
CA B:ASN142 4.2 11.3 1.0
CG B:ASN142 4.3 13.2 1.0
CA B:GLU116 4.3 12.1 1.0
CB B:ASN142 4.4 11.7 1.0
O B:HOH500 4.4 18.8 0.5
CG B:GLU116 4.5 15.0 1.0
O B:HOH423 4.6 22.1 1.0
CE2 B:PHE118 4.7 21.0 1.0
C B:SER141 4.8 11.2 1.0
OE1 B:GLU116 4.9 19.7 1.0
O B:HOH494 4.9 31.6 1.0
O B:GLU116 4.9 11.8 1.0
C B:PHE118 4.9 16.9 1.0
N B:HIS143 5.0 12.8 1.0
N B:ASN142 5.0 10.8 1.0

Reference:

S.H.Light, W.F.Anderson, A.Lavie. Reassessing the Type I Dehydroquinate Dehydratase Catalytic Triad: Kinetic and Structural Studies of GLU86 Mutants. Protein Sci. V. 22 418 2013.
ISSN: ISSN 0961-8368
PubMed: 23341204
DOI: 10.1002/PRO.2218
Page generated: Sat Dec 12 10:40:48 2020

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