Calcium in PDB 6ifi: Crystal Structure of the Apo Form of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae

All present enzymatic activity of Crystal Structure of the Apo Form of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae:
2.7.7.43;

The structure of Crystal Structure of the Apo Form of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae, PDB code: 6ifi 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)	25.08 / 2.80
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	75.250, 75.250, 109.590, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 24

The binding sites of Calcium atom in the Crystal Structure of the Apo Form of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae (pdb code 6ifi). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Apo Form of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae, PDB code: 6ifi:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of the Apo Form of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Apo Form of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:0.2 occ:1.00 O A:HOH414 2.4 87.6 1.0 O A:HOH412 2.7 71.0 1.0 O A:HOH421 2.7 51.0 1.0 O A:HOH430 2.8 61.3 1.0 OE1 A:GLU121 3.7 68.5 1.0 O A:HOH428 4.1 78.2 1.0 OH A:TYR204 4.4 58.4 1.0 CD A:GLU121 4.6 91.3 1.0 NE2 A:HIS118 4.6 52.0 1.0 OE1 A:GLU210 4.6 69.8 1.0 CD2 A:HIS118 4.7 51.8 1.0 OE2 A:GLU121 4.8 98.5 1.0 OE2 A:GLU210 4.8 79.1 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of the Apo Form of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Apo Form of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca301 b:90.8 occ:1.00 O B:HOH432 2.7 62.8 1.0 O B:HOH431 2.7 60.1 1.0 O B:HOH418 2.8 41.7 1.0 O B:HOH425 3.0 62.3 1.0 O B:HOH424 3.0 64.1 1.0 OE1 B:GLU121 3.4 52.4 1.0 OH B:TYR204 3.9 44.6 1.0 O B:HOH421 4.0 68.6 1.0 O B:HOH436 4.3 63.4 1.0 CD B:GLU121 4.4 76.7 1.0 OE2 B:GLU121 4.7 82.2 1.0 O B:VAL205 4.7 49.9 1.0 CD2 B:HIS118 4.8 40.0 1.0 CZ B:TYR204 4.9 44.8 1.0 O B:HOH412 4.9 56.6 1.0 NE2 B:HIS118 4.9 40.1 1.0 OE2 B:GLU210 5.0 45.3 1.0

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