Calcium in PDB 1o8l: Pectate Lyase C From Erwinia Chrysanthemi at pH 4.5 with 5MM CA2+

All present enzymatic activity of Pectate Lyase C From Erwinia Chrysanthemi at pH 4.5 with 5MM CA2+:
4.2.2.2;

The structure of Pectate Lyase C From Erwinia Chrysanthemi at pH 4.5 with 5MM CA2+, PDB code: 1o8l 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 (°)	72.770, 81.020, 95.780, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 21.8

The binding sites of Calcium atom in the Pectate Lyase C From Erwinia Chrysanthemi at pH 4.5 with 5MM CA2+ (pdb code 1o8l). 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 4.5 with 5MM CA2+, PDB code: 1o8l:

Calcium binding site 1 out of 1 in the Pectate Lyase C From Erwinia Chrysanthemi at pH 4.5 with 5MM 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 4.5 with 5MM CA2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1353 b:25.1 occ:0.38 O A:HOH2059 1.9 37.8 0.6 O A:HOH2058 2.3 24.7 0.8 OD1 A:ASP129 2.5 15.5 0.4 OE1 A:GLU166 2.7 30.0 1.0 OD2 A:ASP170 2.7 27.8 1.0 OD1 A:ASP131 2.8 28.6 1.0 OD2 A:ASP131 2.8 27.1 1.0 CG A:ASP131 3.1 24.9 1.0 CD A:GLU166 3.4 26.8 1.0 CG A:ASP129 3.7 16.9 0.1 CG A:ASP170 3.9 23.2 1.0 OE2 A:GLU166 4.0 31.9 1.0 CG A:GLU166 4.1 22.1 1.0 O A:HOH2080 4.1 46.9 1.0 OD2 A:ASP129 4.3 18.3 0.4 OD1 A:ASP129 4.5 22.0 0.6 CB A:ASP131 4.6 21.5 1.0 CB A:ASP170 4.7 16.9 1.0 OD1 A:ASP170 4.8 22.6 1.0 CA A:ASP129 4.8 16.9 1.0 CB A:ASP129 4.8 16.9 0.4 OG A:SER167 4.8 23.8 1.0 CB A:GLU166 4.9 16.9 1.0 CB A:ASP129 4.9 19.1 0.6

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