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Calcium in PDB 5ex2: Crystal Structure of Cyclophilin AQUACYP293 From Hirschia Baltica

Enzymatic activity of Crystal Structure of Cyclophilin AQUACYP293 From Hirschia Baltica

All present enzymatic activity of Crystal Structure of Cyclophilin AQUACYP293 From Hirschia Baltica:
5.2.1.8;

Protein crystallography data

The structure of Crystal Structure of Cyclophilin AQUACYP293 From Hirschia Baltica, PDB code: 5ex2 was solved by R.P.Jakob, T.Maier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.87 / 1.29
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.940, 72.730, 73.930, 90.00, 93.00, 90.00
R / Rfree (%) 16.9 / 19.5

Other elements in 5ex2:

The structure of Crystal Structure of Cyclophilin AQUACYP293 From Hirschia Baltica also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Cyclophilin AQUACYP293 From Hirschia Baltica (pdb code 5ex2). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Cyclophilin AQUACYP293 From Hirschia Baltica, PDB code: 5ex2:

Calcium binding site 1 out of 1 in 5ex2

Go back to Calcium Binding Sites List in 5ex2
Calcium binding site 1 out of 1 in the Crystal Structure of Cyclophilin AQUACYP293 From Hirschia Baltica


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 Cyclophilin AQUACYP293 From Hirschia Baltica within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca301

b:13.3
occ:1.00
 O B:HOH486 2.3 17.9 1.0
O B:HOH788 2.3 16.6 1.0
OE1 B:GLN131 2.4 12.3 1.0
O B:HOH674 2.4 20.1 1.0
OE1 B:GLN113 2.4 14.6 1.0
OE2 B:GLU133 2.5 19.4 1.0
OE1 B:GLU133 2.6 14.6 1.0
CD B:GLU133 2.9 17.5 1.0
CD B:GLN131 3.3 11.5 1.0
CD B:GLN113 3.6 17.5 1.0
HB2 B:GLN113 3.6 19.9 1.0
HE22 B:GLN131 3.8 13.5 1.0
HB3 B:GLN131 3.8 11.4 1.0
H B:ASP132 3.9 11.4 1.0
NE2 B:GLN131 4.0 11.2 1.0
H B:GLU133 4.2 14.6 1.0
O B:HOH789 4.3 37.9 1.0
HE22 B:GLN113 4.3 17.4 1.0
HE1 B:TYR118 4.4 16.0 1.0
CB B:GLN113 4.4 16.6 1.0
HB2 B:ASP132 4.4 12.5 1.0
CG B:GLN131 4.4 10.2 1.0
O B:HOH606 4.4 17.0 1.0
CG B:GLU133 4.4 17.2 1.0
HB3 B:GLN113 4.4 19.9 1.0
NE2 B:GLN113 4.5 14.5 1.0
HA B:GLN131 4.5 11.5 1.0
CB B:GLN131 4.5 9.5 1.0
OD1 B:ASP132 4.5 22.4 1.0
CG B:GLN113 4.6 16.1 1.0
HG3 B:GLN131 4.6 12.2 1.0
N B:ASP132 4.6 9.5 1.0
O B:HOH941 4.6 41.1 1.0
O B:HOH769 4.6 29.8 1.0
O B:HOH801 4.7 25.8 1.0
O B:HOH693 4.7 26.2 1.0
HG2 B:GLU133 4.7 20.6 1.0
HE21 B:GLN131 4.7 13.5 1.0
O B:HOH722 4.8 18.5 1.0
O B:HOH505 4.8 33.0 1.0
HG3 B:GLU133 4.8 20.6 1.0
CE1 B:TYR118 4.8 13.3 1.0
HD1 B:TYR118 4.9 16.0 1.0
CA B:GLN131 5.0 9.6 1.0
HG3 B:GLN113 5.0 19.3 1.0
N B:GLU133 5.0 12.2 1.0

Reference:

R.P.Jakob, P.A.Schmidpeter, J.R.Koch, F.X.Schmid, T.Maier. Structural and Functional Characterization of A Novel Family of Cyclophilins, the Aquacyps. Plos One V. 11 57070 2016.
ISSN: ESSN 1932-6203
PubMed: 27276069
DOI: 10.1371/JOURNAL.PONE.0157070
Page generated: Sun Jul 14 18:54:31 2024

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