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Chlorine in PDB 4mus: Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog

Protein crystallography data

The structure of Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog, PDB code: 4mus was solved by P.J.Stogios, E.Evdokimova, D.Meziane-Cherif, R.Di Leo, V.Yim, P.Courvalin, A.Savchenko, W.F.Anderson, Center For Structural Genomics Ofinfectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.20 / 1.68
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 44.256, 44.780, 62.407, 86.84, 77.29, 64.15
R / Rfree (%) 16.8 / 20.7

Other elements in 4mus:

The structure of Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog (pdb code 4mus). 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 Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog, PDB code: 4mus:

Chlorine binding site 1 out of 1 in 4mus

Go back to Chlorine Binding Sites List in 4mus
Chlorine binding site 1 out of 1 in the Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog


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 Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl206

b:36.5
occ:1.00
NH2 A:ARG69 3.0 20.9 1.0
N B:LEU22 3.2 21.0 1.0
O A:HOH362 3.2 36.6 1.0
CD2 B:HIS21 3.5 36.0 1.0
NE A:ARG69 3.5 19.5 1.0
CA B:HIS21 3.5 28.8 1.0
O B:LEU22 3.5 20.0 1.0
CB B:HIS21 3.6 24.9 1.0
CZ A:ARG69 3.7 20.5 1.0
C B:HIS21 3.8 25.3 1.0
CG B:HIS21 3.8 33.5 1.0
O B:HOH340 4.1 28.5 1.0
CA B:LEU22 4.2 17.9 1.0
C B:LEU22 4.3 18.0 1.0
O A:HOH336 4.4 17.4 0.5
CE A:LYS65 4.6 33.9 1.0
NE2 B:HIS21 4.6 47.0 1.0
CD A:ARG69 4.8 17.0 1.0
O A:HOH506 4.8 40.5 1.0
N B:HIS21 4.8 31.7 1.0
CB B:LEU22 4.9 26.1 1.0
NH1 A:ARG69 5.0 16.6 1.0

Reference:

D.Meziane-Cherif, P.J.Stogios, E.Evdokimova, A.Savchenko, P.Courvalin. Structural Basis For the Evolution of Vancomycin Resistance D,D-Peptidases. Proc.Natl.Acad.Sci.Usa V. 111 5872 2014.
ISSN: ISSN 0027-8424
PubMed: 24711382
DOI: 10.1073/PNAS.1402259111
Page generated: Sat Dec 12 10:56:49 2020

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