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Cadmium in PDB 5yrx: Crystal Structure of A Hypothetical Protein RV3716C From Mycobacterium Tuberculosis

Protein crystallography data

The structure of Crystal Structure of A Hypothetical Protein RV3716C From Mycobacterium Tuberculosis, PDB code: 5yrx was solved by G.Deka, A.Gopalan, M.Prabhavathi, H.S.Savithri, A.Raja, M.R.N.Murthy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.00 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 35.110, 183.750, 37.250, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 21.6

Cadmium Binding Sites:

The binding sites of Cadmium atom in the Crystal Structure of A Hypothetical Protein RV3716C From Mycobacterium Tuberculosis (pdb code 5yrx). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total only one binding site of Cadmium was determined in the Crystal Structure of A Hypothetical Protein RV3716C From Mycobacterium Tuberculosis, PDB code: 5yrx:

Cadmium binding site 1 out of 1 in 5yrx

Go back to Cadmium Binding Sites List in 5yrx
Cadmium binding site 1 out of 1 in the Crystal Structure of A Hypothetical Protein RV3716C From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Crystal Structure of A Hypothetical Protein RV3716C From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd201

b:11.9
occ:0.80
OD2 A:ASP72 2.2 16.1 1.0
OE2 A:GLU68 2.4 15.0 1.0
OD1 A:ASP72 2.7 14.8 1.0
CG A:ASP72 2.8 14.0 1.0
CD A:GLU68 3.4 15.7 1.0
CG A:GLU68 3.6 12.3 1.0
O A:HOH323 4.1 17.5 1.0
CB A:ASP72 4.3 13.6 1.0
O A:HOH315 4.5 25.0 1.0
OE1 A:GLU68 4.5 17.2 1.0
O A:HOH314 4.6 32.9 1.0
O A:GLU68 4.7 11.1 1.0

Reference:

A.Gopalan, G.Deka, M.Prabhavathi, H.S.Savithri, M.R.N.Murthy, A.Raja. Structural and Biophysical Characterization of RV3716C, A Hypothetical Protein From Mycobacterium Tuberculosis Biochem. Biophys. Res. V. 495 982 2018COMMUN..
ISSN: ESSN 1090-2104
PubMed: 29154992
DOI: 10.1016/J.BBRC.2017.11.093
Page generated: Sat Dec 12 08:28:00 2020

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