Calcium in PDB 6e7k: Structure of the Lipoprotein Lipase GPIHBP1 Complex That Mediates Plasma Triglyceride Hydrolysis

All present enzymatic activity of Structure of the Lipoprotein Lipase GPIHBP1 Complex That Mediates Plasma Triglyceride Hydrolysis:
3.1.1.34;

The structure of Structure of the Lipoprotein Lipase GPIHBP1 Complex That Mediates Plasma Triglyceride Hydrolysis, PDB code: 6e7k was solved by G.Birrane, M.Meiyappan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.41 / 2.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	101.948, 153.206, 95.783, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 23.5

The binding sites of Calcium atom in the Structure of the Lipoprotein Lipase GPIHBP1 Complex That Mediates Plasma Triglyceride Hydrolysis (pdb code 6e7k). 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 the Lipoprotein Lipase GPIHBP1 Complex That Mediates Plasma Triglyceride Hydrolysis, PDB code: 6e7k:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of the Lipoprotein Lipase GPIHBP1 Complex That Mediates Plasma Triglyceride Hydrolysis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the Lipoprotein Lipase GPIHBP1 Complex That Mediates Plasma Triglyceride Hydrolysis within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca501 b:98.2 occ:1.00 O A:ALA194 2.4 96.7 1.0 O A:HOH601 2.4 80.1 1.0 O A:HOH602 2.5 79.9 1.0 OD2 A:ASP202 2.5 82.6 1.0 OD1 A:ASP202 2.6 83.2 1.0 O A:ARG197 2.7 81.4 1.0 OG A:SER199 2.7 90.7 1.0 CG A:ASP202 2.9 83.0 1.0 C A:ALA194 3.1 96.4 1.0 OD1 A:ASP201 3.5 98.1 1.0 CB A:SER199 3.6 89.0 1.0 N A:PRO195 3.9 96.0 1.0 C A:ARG197 3.9 83.8 1.0 CA A:ALA194 3.9 97.3 1.0 N A:SER199 3.9 83.9 1.0 CA A:PRO195 4.0 93.8 1.0 CB A:ALA194 4.0 98.8 1.0 C A:PRO195 4.2 92.3 1.0 CA A:SER199 4.3 86.0 1.0 C A:LEU198 4.3 84.0 1.0 O A:PRO195 4.4 91.5 1.0 CB A:ASP202 4.4 82.6 1.0 CG A:ASP201 4.5 98.8 1.0 N A:ARG197 4.5 90.0 1.0 O A:GLY166 4.6 78.2 1.0 OD2 A:ASP201 4.6 0.4 1.0 CA A:LEU198 4.7 80.6 1.0 CB A:SER170 4.7 85.3 1.0 N A:LEU198 4.7 80.6 1.0 N A:SER196 4.8 93.9 1.0 CA A:ARG197 4.9 86.9 1.0 C A:GLY166 4.9 76.8 1.0 O A:LEU198 4.9 85.9 1.0 O A:SER199 5.0 86.6 1.0 C A:SER199 5.0 84.9 1.0

Calcium binding site 2 out of 2 in the Structure of the Lipoprotein Lipase GPIHBP1 Complex That Mediates Plasma Triglyceride Hydrolysis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of the Lipoprotein Lipase GPIHBP1 Complex That Mediates Plasma Triglyceride Hydrolysis within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca505 b:96.5 occ:1.00 O B:HOH602 2.4 72.1 1.0 O B:HOH607 2.4 65.8 1.0 OD2 B:ASP202 2.4 72.2 1.0 O B:ALA194 2.5 80.4 1.0 OD1 B:ASP202 2.6 75.8 1.0 OG B:SER199 2.6 82.5 1.0 O B:ARG197 2.7 71.9 1.0 CG B:ASP202 2.8 74.6 1.0 C B:ALA194 3.2 81.0 1.0 CB B:SER199 3.6 78.5 1.0 N B:SER199 3.8 71.9 1.0 C B:ARG197 3.9 71.3 1.0 N B:PRO195 4.0 80.2 1.0 CA B:ALA194 4.0 83.3 1.0 OD2 B:ASP201 4.0 95.5 1.0 CB B:ALA194 4.0 84.2 1.0 CA B:PRO195 4.1 78.9 1.0 OD1 B:ASP201 4.2 96.2 1.0 CA B:SER199 4.2 75.1 1.0 C B:LEU198 4.3 70.2 1.0 CB B:ASP202 4.3 73.3 1.0 C B:PRO195 4.4 78.2 1.0 CG B:ASP201 4.4 92.8 1.0 O B:GLY166 4.5 75.4 1.0 O B:PRO195 4.6 78.3 1.0 CA B:LEU198 4.6 67.8 1.0 N B:ARG197 4.6 74.9 1.0 CB B:SER170 4.7 75.5 1.0 N B:LEU198 4.7 67.3 1.0 C B:GLY166 4.8 73.0 1.0 O B:SER199 4.8 71.8 1.0 C B:SER199 4.9 74.6 1.0 O B:LEU198 4.9 71.4 1.0 CA B:ARG197 4.9 73.1 1.0 N B:SER196 4.9 79.2 1.0 OG B:SER170 5.0 76.0 1.0

G.Birrane, A.P.Beigneux, B.Dwyer, B.Strack-Logue, K.K.Kristensen, O.L.Francone, L.G.Fong, H.D.T.Mertens, C.Q.Pan, M.Ploug, S.G.Young, M.Meiyappan. Structure of the Lipoprotein Lipase-GPIHBP1 Complex That Mediates Plasma Triglyceride Hydrolysis. Proc. Natl. Acad. Sci. V. 116 1723 2019U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30559189
DOI: 10.1073/PNAS.1817984116