Calcium in PDB 1o8e: Pectate Lyase C From Erwinia Chrysanthemi at pH 11.2 with 1MM CA2+

All present enzymatic activity of Pectate Lyase C From Erwinia Chrysanthemi at pH 11.2 with 1MM CA2+:
4.2.2.2;

The structure of Pectate Lyase C From Erwinia Chrysanthemi at pH 11.2 with 1MM CA2+, PDB code: 1o8e was solved by S.R.Herron, F.A.Jurnak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.480, 76.760, 91.870, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 24.2

The binding sites of Calcium atom in the Pectate Lyase C From Erwinia Chrysanthemi at pH 11.2 with 1MM CA2+ (pdb code 1o8e). 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 Pectate Lyase C From Erwinia Chrysanthemi at pH 11.2 with 1MM CA2+, PDB code: 1o8e:

Calcium binding site 1 out of 1 in the Pectate Lyase C From Erwinia Chrysanthemi at pH 11.2 with 1MM CA2+


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Pectate Lyase C From Erwinia Chrysanthemi at pH 11.2 with 1MM CA2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1353 b:31.5 occ:0.42 OD1 A:ASP131 2.4 30.8 1.0 OD2 A:ASP170 2.6 26.3 1.0 OE1 A:GLU166 2.7 31.4 1.0 OD2 A:ASP131 2.8 30.9 1.0 O A:HOH2083 2.9 50.1 1.0 CG A:ASP131 3.0 27.0 1.0 O A:HOH2102 3.1 40.3 1.0 CD A:GLU166 3.1 30.2 1.0 OE2 A:GLU166 3.3 33.5 1.0 O A:HOH2101 3.5 48.9 1.0 CG A:ASP170 3.7 23.6 1.0 OD1 A:ASP129 3.7 30.3 0.6 OG A:SER167 4.3 36.2 1.0 CB A:ASP170 4.3 23.0 1.0 CG A:GLU166 4.3 28.4 1.0 CB A:SER167 4.3 31.1 1.0 O A:HOH2103 4.3 0.0 1.0 CB A:ASP131 4.5 26.2 1.0 N A:SER167 4.6 28.9 1.0 OD1 A:ASP170 4.6 23.6 1.0 CB A:GLU166 4.8 29.5 1.0 CG A:ASP129 4.9 30.2 0.1 CD A:ARG134 4.9 27.3 1.0

S.R.Herron, R.Scavetta, M.Garrett, M.Legner, F.A.Jurnak. Characterization and Implications of CA2+ Binding to Pectate Lyase C J.Biol.Chem. V. 278 12271 2003.
ISSN: ISSN 0021-9258
PubMed: 12540845
DOI: 10.1074/JBC.M209306200