Calcium in PDB 3b90: Crystal Structure of the Catalytic Domain of Pectate Lyase Peli From Erwinia Chrysanthemi

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Pectate Lyase Peli From Erwinia Chrysanthemi:
4.2.2.2;

The structure of Crystal Structure of the Catalytic Domain of Pectate Lyase Peli From Erwinia Chrysanthemi, PDB code: 3b90 was solved by C.Creze, S.Castang, E.Derivery, R.Haser, V.Shevchik, P.Gouet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.83 / 2.11
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.400, 62.600, 128.100, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 27.3

The structure of Crystal Structure of the Catalytic Domain of Pectate Lyase Peli From Erwinia Chrysanthemi also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Calcium atom in the Crystal Structure of the Catalytic Domain of Pectate Lyase Peli From Erwinia Chrysanthemi (pdb code 3b90). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Catalytic Domain of Pectate Lyase Peli From Erwinia Chrysanthemi, PDB code: 3b90:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of Pectate Lyase Peli From Erwinia Chrysanthemi


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 the Catalytic Domain of Pectate Lyase Peli From Erwinia Chrysanthemi within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca701 b:30.4 occ:1.00 O A:HOH1148 2.2 11.6 1.0 OD1 A:ASN213 2.2 21.3 1.0 O A:ILE192 2.3 17.1 1.0 O A:TYR218 2.3 25.4 1.0 OD1 A:ASP191 2.5 19.6 1.0 O A:HOH1147 2.5 32.5 1.0 CG A:ASN213 3.4 21.3 1.0 C A:TYR218 3.5 25.6 1.0 C A:ILE192 3.5 16.8 1.0 CG A:ASP191 3.6 19.9 1.0 N A:TYR218 3.9 25.4 1.0 ND2 A:ASN213 4.0 21.0 1.0 OD2 A:ASP191 4.1 21.0 1.0 N A:ILE192 4.2 16.4 1.0 CA A:TYR218 4.2 26.3 1.0 C A:ASP191 4.3 16.4 1.0 CA A:ILE192 4.3 16.4 1.0 O A:CYS193 4.4 17.5 1.0 N A:ALA214 4.5 23.0 1.0 C A:GLY217 4.5 25.1 1.0 N A:CYS193 4.5 16.8 1.0 N A:GLY219 4.5 26.6 1.0 O A:GLY220 4.5 26.9 1.0 O A:ASP191 4.5 16.8 1.0 O A:ALA214 4.5 25.9 1.0 CB A:ASN213 4.6 19.9 1.0 CA A:CYS193 4.6 16.2 1.0 CA A:ASN213 4.6 19.1 1.0 CA A:GLY219 4.7 26.0 1.0 CB A:ASP191 4.7 16.4 1.0 CB A:ILE192 4.7 15.5 1.0 CA A:GLY217 4.8 24.9 1.0 CA A:ASP191 4.8 16.0 1.0 CB A:TYR218 4.9 27.4 1.0 C A:GLY219 4.9 26.1 1.0 C A:CYS193 5.0 17.0 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of Pectate Lyase Peli From Erwinia Chrysanthemi


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Catalytic Domain of Pectate Lyase Peli From Erwinia Chrysanthemi within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca702 b:28.4 occ:1.00 O B:TYR218 2.3 33.7 1.0 OD1 B:ASN213 2.3 24.1 1.0 O B:ILE192 2.3 12.0 1.0 OD1 B:ASP191 2.5 17.9 1.0 CG B:ASP191 3.4 16.9 1.0 CG B:ASN213 3.5 25.0 1.0 C B:TYR218 3.5 34.0 1.0 C B:ILE192 3.5 12.7 1.0 OD2 B:ASP191 3.9 21.0 1.0 O B:ALA214 4.0 32.7 1.0 N B:ALA214 4.1 26.9 1.0 N B:ILE192 4.1 14.3 1.0 ND2 B:ASN213 4.1 28.4 1.0 N B:TYR218 4.1 35.1 1.0 CA B:TYR218 4.3 34.7 1.0 C B:ASP191 4.3 14.4 1.0 CA B:ILE192 4.3 11.9 1.0 O B:GLY220 4.4 38.0 1.0 N B:GLY219 4.5 34.0 1.0 C B:GLY217 4.5 36.4 1.0 N B:CYS193 4.6 13.2 1.0 CA B:ASN213 4.6 21.6 1.0 CB B:ASN213 4.6 21.8 1.0 CB B:ASP191 4.6 15.7 1.0 O B:ASP191 4.6 15.9 1.0 CB B:TYR218 4.6 35.0 1.0 CA B:GLY219 4.7 35.4 1.0 CB B:ILE192 4.7 12.1 1.0 O B:CYS193 4.7 13.9 1.0 CA B:CYS193 4.7 13.5 1.0 CA B:ASP191 4.8 15.7 1.0 C B:ASN213 4.8 22.6 1.0 O B:GLY217 4.9 34.9 1.0 C B:ALA214 4.9 32.3 1.0 CA B:ALA214 4.9 30.0 1.0 N B:GLY220 5.0 36.5 1.0

C.Creze, S.Castang, E.Derivery, R.Haser, N.Hugouvieux-Cotte-Pattat, V.E.Shevchik, P.Gouet. The Crystal Structure of Pectate Lyase Peli From Soft Rot Pathogen Erwinia Chrysanthemi in Complex with Its Substrate J.Biol.Chem. V. 283 18260 2008.
ISSN: ISSN 0021-9258
PubMed: 18430740
DOI: 10.1074/JBC.M709931200