Calcium in PDB 1oil: Structure of Lipase

All present enzymatic activity of Structure of Lipase:
3.1.1.3;

The structure of Structure of Lipase, PDB code: 1oil was solved by K.K.Kim, H.K.Song, D.H.Shin, S.W.Suh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	85.230, 47.420, 86.530, 90.00, 116.11, 90.00
R / Rfree (%)	18 / 25.5

The binding sites of Calcium atom in the Structure of Lipase (pdb code 1oil). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of Lipase, PDB code: 1oil:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of Lipase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Lipase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:10.5 occ:1.00 O A:HOH507 2.3 3.0 1.0 O A:HOH538 2.3 10.3 1.0 O A:VAL296 2.4 14.7 1.0 OD2 A:ASP242 2.4 8.4 1.0 OD1 A:ASP288 2.4 9.9 1.0 O A:GLN292 2.8 20.3 1.0 CG A:ASP242 3.6 9.8 1.0 C A:VAL296 3.6 14.7 1.0 CG A:ASP288 3.6 10.0 1.0 C A:GLN292 4.0 23.6 1.0 CA A:ARG297 4.1 15.2 1.0 ND2 A:ASN285 4.2 17.1 1.0 N A:ARG297 4.2 13.7 1.0 OG A:SER244 4.3 16.2 1.0 CA A:ASP288 4.4 10.1 1.0 OD1 A:ASP242 4.4 10.0 1.0 CB A:ASP242 4.4 5.3 1.0 N A:ASP288 4.4 7.4 1.0 OD2 A:ASP288 4.4 8.1 1.0 OG1 A:THR245 4.4 15.1 1.0 OD1 A:ASN285 4.4 21.1 1.0 O A:HOH523 4.5 24.8 1.0 CB A:ARG297 4.6 18.7 1.0 CB A:ASP288 4.6 9.3 1.0 CA A:VAL296 4.7 14.9 1.0 C A:LEU287 4.8 8.2 1.0 CG A:ASN285 4.8 13.4 1.0 CB A:VAL296 4.8 15.7 1.0 N A:VAL296 4.9 14.0 1.0 O A:LEU287 4.9 11.0 1.0 CB A:LEU287 5.0 8.9 1.0

Calcium binding site 2 out of 2 in the Structure of Lipase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of Lipase within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca401 b:11.7 occ:1.00 O B:HOH705 2.3 7.0 1.0 O B:VAL296 2.3 15.1 1.0 OD1 B:ASP288 2.3 8.4 1.0 O B:HOH736 2.4 17.2 1.0 OD2 B:ASP242 2.4 14.2 1.0 O B:GLN292 2.9 23.5 1.0 C B:VAL296 3.5 12.5 1.0 CG B:ASP242 3.5 11.9 1.0 CG B:ASP288 3.5 8.3 1.0 CA B:ARG297 4.1 13.1 1.0 C B:GLN292 4.1 24.5 1.0 N B:ARG297 4.2 11.9 1.0 ND2 B:ASN285 4.3 13.7 1.0 OD2 B:ASP288 4.3 6.4 1.0 CA B:ASP288 4.3 8.9 1.0 OD1 B:ASP242 4.3 11.0 1.0 CB B:ASP242 4.3 9.1 1.0 OD1 B:ASN285 4.4 16.1 1.0 N B:ASP288 4.4 5.0 1.0 O B:HOH721 4.4 20.5 1.0 OG1 B:THR245 4.5 16.8 1.0 OG B:SER244 4.5 16.8 1.0 CB B:ASP288 4.5 8.3 1.0 CB B:ARG297 4.6 14.1 1.0 CA B:VAL296 4.7 12.5 1.0 CG B:ASN285 4.8 10.6 1.0 C B:LEU287 4.8 3.8 1.0 CB B:VAL296 4.8 13.2 1.0 N B:VAL296 4.9 12.5 1.0 CB B:LEU293 4.9 30.6 1.0

K.K.Kim, H.K.Song, D.H.Shin, K.Y.Hwang, S.W.Suh. The Crystal Structure of A Triacylglycerol Lipase From Pseudomonas Cepacia Reveals A Highly Open Conformation in the Absence of A Bound Inhibitor. Structure V. 5 173 1997.
ISSN: ISSN 0969-2126
PubMed: 9032073
DOI: 10.1016/S0969-2126(97)00177-9