Calcium in PDB 2btw: Crystal Structure of ALR0975

All present enzymatic activity of Crystal Structure of ALR0975:
2.3.2.15;

The structure of Crystal Structure of ALR0975, PDB code: 2btw was solved by D.Vivares, P.Arnoux, D.Pignol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.10 / 2.0
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.860, 62.467, 76.552, 90.00, 101.38, 90.00
R / Rfree (%)	20 / 25.7

The binding sites of Calcium atom in the Crystal Structure of ALR0975 (pdb code 2btw). 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 ALR0975, PDB code: 2btw:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of ALR0975


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 ALR0975 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca400 b:28.5 occ:1.00 O A:ASN165 2.1 19.3 1.0 O A:ASN159 2.2 18.7 1.0 O A:GLN162 2.4 25.8 1.0 OD1 A:ASP53 2.4 22.1 1.0 OD2 A:ASP53 2.7 19.6 1.0 CG A:ASP53 2.9 17.4 1.0 C A:ASN165 3.2 18.8 1.0 C A:ASN159 3.3 20.0 1.0 C A:GLN162 3.5 26.1 1.0 CB A:ASN165 3.7 19.8 1.0 CA A:ASN165 3.8 19.8 1.0 CA A:LEU160 3.9 19.5 1.0 N A:GLN162 3.9 24.9 1.0 N A:ASN165 4.0 19.9 1.0 N A:LEU160 4.0 19.0 1.0 C A:LEU160 4.1 20.8 1.0 CA A:GLN162 4.1 25.6 1.0 N A:PHE166 4.2 15.5 1.0 CA A:ASN159 4.3 20.9 1.0 CB A:GLN162 4.3 25.9 1.0 O A:LEU160 4.3 21.6 1.0 CB A:ASP53 4.4 13.4 1.0 O A:HOH2014 4.4 32.9 1.0 CA A:PHE166 4.5 14.7 1.0 N A:ASP163 4.6 25.9 1.0 N A:LYS161 4.6 22.6 1.0 ND2 A:ASN159 4.6 27.7 1.0 CB A:ASN159 4.7 21.1 1.0 CA A:ASP163 4.7 26.5 1.0 C A:ASP163 4.8 25.3 1.0 C A:LYS161 4.9 24.1 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of ALR0975


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 ALR0975 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca400 b:33.0 occ:1.00 O B:ASN159 2.2 17.9 1.0 O B:ASN165 2.3 19.1 1.0 OD1 B:ASP53 2.4 19.1 1.0 O B:GLN162 2.5 25.7 1.0 OD2 B:ASP53 2.6 17.7 1.0 CG B:ASP53 2.9 14.6 1.0 C B:ASN159 3.2 19.7 1.0 C B:ASN165 3.2 17.5 1.0 CB B:ASN165 3.6 18.6 1.0 C B:GLN162 3.6 24.9 1.0 CA B:ASN165 3.9 18.4 1.0 CA B:LEU160 3.9 19.7 1.0 N B:LEU160 4.0 19.0 1.0 N B:GLN162 4.0 23.9 1.0 N B:ASN165 4.0 16.8 1.0 C B:LEU160 4.1 20.8 1.0 CA B:GLN162 4.1 25.0 1.0 N B:PHE166 4.2 14.6 1.0 CA B:ASN159 4.2 20.0 1.0 O B:LEU160 4.2 21.7 1.0 CB B:GLN162 4.3 24.6 1.0 CB B:ASP53 4.4 12.4 1.0 CA B:PHE166 4.4 14.2 1.0 CB B:ASN159 4.5 20.5 1.0 N B:ASP163 4.7 24.4 1.0 N B:LYS161 4.7 22.1 1.0 O B:HOH2100 4.8 43.2 1.0 CG B:ASN165 4.9 23.3 1.0 C B:ASP163 5.0 22.4 1.0 C B:LYS161 5.0 23.0 1.0

D.Vivares, P.Arnoux, D.Pignol. A Papain-Like Enzyme at Work: Native and Acyl- Enzyme Intermediate Structures in Phytochelatin Synthesis. Proc.Natl.Acad.Sci.Usa V. 102 18848 2005.
ISSN: ISSN 0027-8424
PubMed: 16339904
DOI: 10.1073/PNAS.0505833102