Magnesium in PDB 6ifd: Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+.

Enzymatic activity of Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+.

All present enzymatic activity of Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+.:
2.7.7.43;

Protein crystallography data

The structure of Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+., PDB code: 6ifd was solved by S.Bose, R.Subramanian, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.55 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 93.380, 97.720, 98.760, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 24

Other elements in 6ifd:

The structure of Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+. also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+. (pdb code 6ifd). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+., PDB code: 6ifd:

Magnesium binding site 1 out of 1 in 6ifd

Go back to Magnesium Binding Sites List in 6ifd
Magnesium binding site 1 out of 1 in the Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg302

b:64.0
occ:1.00
 O C:HOH427 2.2 59.9 1.0
O C:HOH437 2.3 80.5 1.0
OD1 C:ASP215 2.3 82.7 1.0
O C:HOH417 2.5 72.0 1.0
O2A C:CDP301 2.6 52.5 1.0
CG C:ASP215 3.1 79.4 1.0
OD2 C:ASP215 3.1 87.5 1.0
PA C:CDP301 3.9 51.8 1.0
OD1 C:ASP213 4.0 92.3 1.0
O1A C:CDP301 4.1 55.7 1.0
NZ C:LYS21 4.1 67.7 1.0
OD2 C:ASP213 4.3 96.7 1.0
O C:HOH470 4.4 70.0 1.0
CG C:ASP213 4.5 88.6 1.0
CB C:ASP215 4.5 58.0 1.0
O3A C:CDP301 4.7 52.8 1.0
O C:ILE214 4.8 57.5 1.0
C5' C:CDP301 5.0 50.1 1.0
O5' C:CDP301 5.0 53.7 1.0

Reference:

S.Bose, D.Purkait, D.Joseph, V.Nayak, R.Subramanian. Structural and Functional Characterization of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae. Acta Crystallogr D Struct V. 75 564 2019BIOL.
ISSN: ISSN 2059-7983
PubMed: 31205019
DOI: 10.1107/S2059798319006831
Page generated: Mon Dec 14 22:57:06 2020

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