Calcium in PDB 7cog: Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form)

The structure of Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form), PDB code: 7cog was solved by Y.Yasutake, T.Tamura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.50 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	186.292, 47.092, 70.082, 90.00, 90.05, 90.00
R / Rfree (%)	21.9 / 25.2

The binding sites of Calcium atom in the Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form) (pdb code 7cog). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form), PDB code: 7cog:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:19.6 occ:1.00 OD1 A:ASP288 2.4 13.6 1.0 OD2 A:ASP242 2.4 14.3 1.0 O A:HOH518 2.4 13.9 1.0 O A:HOH520 2.4 11.6 1.0 O A:VAL296 2.4 13.3 1.0 O A:GLN292 2.5 13.7 1.0 C A:GLN292 3.4 13.6 1.0 CG A:ASP288 3.5 13.3 1.0 N A:LEU293 3.6 13.1 1.0 CG A:ASP242 3.6 13.2 1.0 C A:VAL296 3.6 11.2 1.0 CA A:ARG297 3.9 11.2 1.0 O A:HOH508 4.0 13.2 1.0 ND2 A:ASN285 4.2 12.0 1.0 OD2 A:ASP288 4.2 13.3 1.0 N A:ARG297 4.2 11.2 1.0 OD1 A:ASN285 4.2 14.5 1.0 CB A:ASP242 4.3 14.5 1.0 OG1 A:THR245 4.4 14.4 1.0 CA A:ASP288 4.4 12.8 1.0 CB A:ARG297 4.4 13.2 1.0 N A:ASP288 4.4 12.1 1.0 OG A:SER244 4.4 15.6 1.0 CB A:ASP288 4.5 12.6 1.0 OD1 A:ASP242 4.5 16.1 1.0 CG1 A:ILE287 4.6 13.6 1.0 CG A:ASN285 4.6 12.7 1.0 CA A:VAL296 4.8 12.8 1.0 CA A:GLN292 4.8 13.2 1.0 C A:ILE287 4.9 11.7 1.0 O A:ILE287 4.9 12.9 1.0

Calcium binding site 2 out of 4 in the Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca401 b:41.0 occ:1.00 OD1 B:ASP288 2.4 38.2 1.0 OD2 B:ASP242 2.4 39.8 1.0 O B:VAL296 2.5 40.2 1.0 O B:GLN292 2.7 33.5 1.0 O B:HOH506 2.7 43.0 1.0 CG B:ASP242 3.5 36.0 1.0 CG B:ASP288 3.5 36.6 1.0 C B:VAL296 3.5 40.4 1.0 C B:GLN292 3.6 35.5 1.0 N B:LEU293 3.8 37.2 1.0 CA B:ARG297 3.9 37.9 1.0 OG1 B:THR245 4.0 37.7 1.0 ND2 B:ASN285 4.0 38.4 1.0 OD2 B:ASP288 4.1 33.8 1.0 N B:ARG297 4.1 39.3 1.0 OD1 B:ASN285 4.1 37.8 1.0 OD1 B:ASP242 4.2 32.5 1.0 CB B:ASP242 4.3 40.0 1.0 OG B:SER244 4.4 35.6 1.0 CA B:ASP288 4.4 31.6 1.0 N B:ASP288 4.5 32.1 1.0 CG B:ASN285 4.5 36.4 1.0 CB B:ARG297 4.5 38.1 1.0 CB B:ASP288 4.6 41.1 1.0 CA B:VAL296 4.7 39.7 1.0 O B:HOH501 4.8 37.4 1.0 CG1 B:ILE287 4.9 37.2 1.0 CB B:VAL296 4.9 39.3 1.0 C B:ILE287 4.9 34.5 1.0 O B:ILE287 4.9 36.9 1.0 C B:ARG297 4.9 40.8 1.0 CG1 B:VAL296 5.0 36.3 1.0 CA B:GLN292 5.0 35.6 1.0

Calcium binding site 3 out of 4 in the Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form) within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca401 b:17.5 occ:1.00 OD1 C:ASP288 2.3 18.5 1.0 O C:VAL296 2.3 15.0 1.0 O C:GLN292 2.4 16.2 1.0 OD2 C:ASP242 2.4 18.8 1.0 O C:HOH508 2.4 16.4 1.0 O C:HOH511 2.6 18.1 1.0 C C:GLN292 3.3 16.6 1.0 CG C:ASP288 3.4 16.0 1.0 N C:LEU293 3.5 16.9 1.0 C C:VAL296 3.5 16.6 1.0 CG C:ASP242 3.6 15.7 1.0 OD2 C:ASP288 4.0 17.2 1.0 CA C:ARG297 4.1 19.8 1.0 N C:ARG297 4.2 18.6 1.0 CA C:ASP288 4.3 14.9 1.0 OD1 C:ASN285 4.3 19.1 1.0 CB C:ASP242 4.3 18.2 1.0 OG C:SER244 4.3 12.9 1.0 ND2 C:ASN285 4.4 18.4 1.0 O C:HOH515 4.4 20.3 1.0 CB C:ASP288 4.4 14.9 1.0 OG1 C:THR245 4.5 17.5 1.0 N C:ASP288 4.5 15.7 1.0 OD1 C:ASP242 4.6 15.6 1.0 CB C:ARG297 4.6 20.3 1.0 CA C:VAL296 4.6 19.6 1.0 CA C:GLN292 4.7 17.8 1.0 CG1 C:ILE287 4.8 18.5 1.0 CG C:ASN285 4.8 15.9 1.0 CB C:VAL296 4.8 19.6 1.0 CA C:LEU293 4.9 16.4 1.0 N C:VAL296 4.9 22.0 1.0 O C:ILE287 4.9 15.8 1.0 C C:ILE287 4.9 15.2 1.0 N C:GLN292 5.0 17.0 1.0

Calcium binding site 4 out of 4 in the Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Cholesterol Esterase From Burkholderia Stabilis (Monoclinic Crystal Form) within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca401 b:25.1 occ:1.00 OD1 D:ASP288 2.3 32.9 1.0 OD2 D:ASP242 2.4 25.3 1.0 O D:VAL296 2.5 27.0 1.0 O D:HOH504 2.5 24.1 1.0 O D:HOH516 2.5 26.5 1.0 O D:GLN292 2.6 28.5 1.0 CG D:ASP242 3.4 28.6 1.0 C D:GLN292 3.4 31.3 1.0 CG D:ASP288 3.5 30.9 1.0 C D:VAL296 3.5 25.3 1.0 N D:LEU293 3.6 28.8 1.0 CA D:ARG297 3.9 26.2 1.0 OD1 D:ASP242 4.1 27.9 1.0 OD2 D:ASP288 4.1 30.6 1.0 N D:ARG297 4.1 25.9 1.0 CB D:ASP242 4.2 28.1 1.0 ND2 D:ASN285 4.3 28.7 1.0 OD1 D:ASN285 4.3 28.6 1.0 OG1 D:THR245 4.3 28.9 1.0 CA D:ASP288 4.4 31.0 1.0 CB D:ARG297 4.4 30.4 1.0 OG D:SER244 4.5 27.7 1.0 CB D:ASP288 4.5 31.1 1.0 N D:ASP288 4.6 28.9 1.0 CA D:VAL296 4.6 30.8 1.0 O D:HOH515 4.7 31.3 1.0 CG D:ASN285 4.7 31.2 1.0 CB D:VAL296 4.8 31.7 1.0 CA D:GLN292 4.9 28.2 1.0 CG1 D:VAL296 4.9 27.5 1.0 CA D:LEU293 5.0 27.6 1.0

Y.Yasutake, K.Konishi, S.Muramatsu, K.Yoshida, S.Aburatani, S.I.Sakasegawa, T.Tamura. Bacterial Triacylglycerol Lipase Is A Potential Cholesterol Esterase: Identification of A Key Determinant For Sterol-Binding Specificity. Int.J.Biol.Macromol. V. 167 578 2021.
ISSN: ISSN 0141-8130
DOI: 10.1016/J.IJBIOMAC.2020.11.184