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Calcium in PDB 2oxe: Structure of the Human Pancreatic Lipase-Related Protein 2

Enzymatic activity of Structure of the Human Pancreatic Lipase-Related Protein 2

All present enzymatic activity of Structure of the Human Pancreatic Lipase-Related Protein 2:
3.1.1.3;

Protein crystallography data

The structure of Structure of the Human Pancreatic Lipase-Related Protein 2, PDB code: 2oxe was solved by J.R.Walker, T.Davis, A.Seitova, P.J.Finerty Jr., C.Butler-Cole, I.Kozieradzki, J.Weigelt, M.Sundstrom, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, S.Dhe-Paganon, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.88 / 2.80
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 216.922, 216.922, 123.618, 90.00, 90.00, 90.00
R / Rfree (%) 22.2 / 26.1

Other elements in 2oxe:

The structure of Structure of the Human Pancreatic Lipase-Related Protein 2 also contains other interesting chemical elements:

Chlorine (Cl) 5 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of the Human Pancreatic Lipase-Related Protein 2 (pdb code 2oxe). 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 Human Pancreatic Lipase-Related Protein 2, PDB code: 2oxe:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2oxe

Go back to Calcium Binding Sites List in 2oxe
Calcium binding site 1 out of 2 in the Structure of the Human Pancreatic Lipase-Related Protein 2


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 Human Pancreatic Lipase-Related Protein 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca600

b:40.8
occ:1.00
OD2 A:ASP211 2.3 40.8 1.0
O A:ARG209 2.4 43.4 1.0
O A:GLU206 2.4 45.3 1.0
OD1 A:ASP214 2.7 47.9 1.0
OD2 A:ASP214 2.7 47.7 1.0
O A:HOH617 2.7 60.6 1.0
CG A:ASP214 3.1 47.2 1.0
CG A:ASP211 3.6 44.1 1.0
C A:ARG209 3.6 44.0 1.0
C A:GLU206 3.7 45.8 1.0
N A:ASP211 4.2 44.5 1.0
O A:GLU207 4.3 45.7 1.0
N A:ARG209 4.4 44.8 1.0
C A:GLU207 4.4 45.7 1.0
OD1 A:ASP211 4.4 45.5 1.0
CA A:LEU210 4.4 44.5 1.0
C A:LEU210 4.4 44.8 1.0
CB A:ALA178 4.4 41.0 1.0
O A:ALA178 4.5 41.8 1.0
N A:LEU210 4.5 44.2 1.0
CB A:ASP214 4.5 47.6 1.0
CB A:ASP211 4.6 44.8 1.0
N A:GLU207 4.6 46.4 1.0
CA A:GLU206 4.6 46.4 1.0
CA A:GLU207 4.6 46.2 1.0
CA A:ARG209 4.6 44.6 1.0
CB A:ARG182 4.8 43.4 1.0
CB A:GLU206 4.8 46.5 1.0
C A:ALA178 4.9 41.8 1.0
N A:VAL208 4.9 45.8 1.0
CD A:ARG182 4.9 44.3 1.0
CA A:ASP211 4.9 44.8 1.0

Calcium binding site 2 out of 2 in 2oxe

Go back to Calcium Binding Sites List in 2oxe
Calcium binding site 2 out of 2 in the Structure of the Human Pancreatic Lipase-Related Protein 2


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 Human Pancreatic Lipase-Related Protein 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca600

b:67.2
occ:1.00
O B:GLU206 2.3 55.8 1.0
OD2 B:ASP211 2.3 47.7 1.0
O B:ARG209 2.4 49.1 1.0
OD1 B:ASP214 2.6 60.7 1.0
OD2 B:ASP214 2.8 56.9 1.0
CG B:ASP214 3.1 58.3 1.0
C B:GLU206 3.5 56.8 1.0
CG B:ASP211 3.6 51.3 1.0
C B:ARG209 3.6 48.0 1.0
N B:ASP211 4.1 47.9 1.0
C B:GLU207 4.2 55.5 1.0
O B:GLU207 4.2 55.5 1.0
CA B:GLU207 4.2 57.5 1.0
N B:GLU207 4.3 57.5 1.0
N B:ARG209 4.3 50.0 1.0
O B:ALA178 4.4 52.5 1.0
OD1 B:ASP211 4.5 53.8 1.0
CA B:LEU210 4.5 46.1 1.0
CB B:ASP211 4.5 50.8 1.0
N B:LEU210 4.5 46.8 1.0
CA B:GLU206 4.5 58.0 1.0
C B:LEU210 4.6 47.1 1.0
CB B:ASP214 4.6 58.2 1.0
CA B:ARG209 4.6 48.4 1.0
CB B:ALA178 4.6 49.0 1.0
N B:VAL208 4.7 54.1 1.0
CB B:ARG182 4.7 56.1 1.0
CD B:ARG182 4.7 56.2 1.0
CA B:ASP211 4.9 49.5 1.0
CB B:GLU206 4.9 59.7 1.0
C B:ALA178 5.0 51.6 1.0
CG B:ARG182 5.0 56.8 1.0

Reference:

C.Eydoux, S.Spinelli, T.L.Davis, J.R.Walker, A.Seitova, S.Dhe-Paganon, A.De Caro, C.Cambillau, F.Carriere. Structure of Human Pancreatic Lipase-Related Protein 2 with the Lid in An Open Conformation. Biochemistry V. 47 9553 2008.
ISSN: ISSN 0006-2960
PubMed: 18702514
DOI: 10.1021/BI8005576
Page generated: Sat Dec 12 03:49:11 2020

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