Barium in PDB 2w2f: Crystal Structure of Single Point Mutant ARG48GLN of P- Coumaric Acid Decarboxylase From Lactobacillus Plantarum Structural Insights Into the Active Site and Decarboxylation Catalytic Mechanism

The structure of Crystal Structure of Single Point Mutant ARG48GLN of P- Coumaric Acid Decarboxylase From Lactobacillus Plantarum Structural Insights Into the Active Site and Decarboxylation Catalytic Mechanism, PDB code: 2w2f was solved by H.Rodriguez, I.Angulo, B.De Las Rivas, N.Campillo, J.A.Paez, R.Munoz, J.M.Mancheno, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.76 / 1.73
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.248, 94.924, 106.722, 90.00, 100.51, 90.00
R / Rfree (%)	22.6 / 27.3

The binding sites of Barium atom in the Crystal Structure of Single Point Mutant ARG48GLN of P- Coumaric Acid Decarboxylase From Lactobacillus Plantarum Structural Insights Into the Active Site and Decarboxylation Catalytic Mechanism (pdb code 2w2f). This binding sites where shown within 5.0 Angstroms radius around Barium atom.
In total 2 binding sites of Barium where determined in the Crystal Structure of Single Point Mutant ARG48GLN of P- Coumaric Acid Decarboxylase From Lactobacillus Plantarum Structural Insights Into the Active Site and Decarboxylation Catalytic Mechanism, PDB code: 2w2f:
Jump to Barium binding site number: 1; 2;

Barium binding site 1 out of 2 in the Crystal Structure of Single Point Mutant ARG48GLN of P- Coumaric Acid Decarboxylase From Lactobacillus Plantarum Structural Insights Into the Active Site and Decarboxylation Catalytic Mechanism


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 1 of Crystal Structure of Single Point Mutant ARG48GLN of P- Coumaric Acid Decarboxylase From Lactobacillus Plantarum Structural Insights Into the Active Site and Decarboxylation Catalytic Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ B:Ba1177 b:7.2 occ:1.00 O B:LEU12 2.7 3.6 1.0 O B:ASP9 2.8 5.0 1.0 O B:HOH2100 2.8 7.7 1.0 O B:HOH2012 2.8 2.8 1.0 O B:HOH2101 2.8 2.2 1.0 O B:ASP10 2.9 3.8 1.0 C B:ASP10 3.6 4.5 1.0 C B:ASP9 3.9 5.5 1.0 C B:LEU12 3.9 3.6 1.0 CA B:ASP10 3.9 4.7 1.0 NZ B:LYS3 4.0 23.6 1.0 OD1 B:ASP142 4.4 6.5 1.0 N B:ASP10 4.4 4.8 1.0 N B:PHE11 4.6 3.8 1.0 N B:LEU12 4.6 3.5 1.0 C B:PHE11 4.7 3.8 1.0 O B:HOH2014 4.7 67.0 1.0 CA B:LEU12 4.8 3.2 1.0 N B:GLY13 4.8 3.3 1.0 OG1 B:THR14 4.8 2.6 1.0 CA B:GLY13 4.9 3.5 1.0 OD1 B:ASP9 4.9 6.8 1.0 CG B:ASP142 4.9 5.7 1.0 O B:PHE11 4.9 3.6 1.0 OD2 B:ASP142 5.0 5.7 1.0

Barium binding site 2 out of 2 in the Crystal Structure of Single Point Mutant ARG48GLN of P- Coumaric Acid Decarboxylase From Lactobacillus Plantarum Structural Insights Into the Active Site and Decarboxylation Catalytic Mechanism


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 2 of Crystal Structure of Single Point Mutant ARG48GLN of P- Coumaric Acid Decarboxylase From Lactobacillus Plantarum Structural Insights Into the Active Site and Decarboxylation Catalytic Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ D:Ba1177 b:5.9 occ:1.00 O D:HOH2014 2.6 7.6 1.0 O D:LEU12 2.7 3.2 1.0 O D:HOH2109 2.9 5.1 1.0 O D:HOH2112 2.9 6.2 1.0 O D:ASP9 2.9 4.7 1.0 O D:ASP10 2.9 4.0 1.0 O D:HOH2110 3.0 7.6 1.0 C D:ASP10 3.6 4.2 1.0 C D:LEU12 4.0 3.4 1.0 C D:ASP9 4.0 4.9 1.0 CA D:ASP10 4.0 4.2 1.0 NZ D:LYS3 4.3 21.0 1.0 OD1 D:ASP142 4.4 6.1 1.0 N D:PHE11 4.5 3.7 1.0 N D:ASP10 4.5 4.6 1.0 N D:LEU12 4.6 3.5 1.0 C D:PHE11 4.7 3.7 1.0 O D:HOH2002 4.7 22.7 1.0 OD1 D:ASP9 4.7 5.3 1.0 OD2 D:ASP142 4.8 3.5 1.0 CA D:LEU12 4.8 3.6 1.0 CG D:ASP142 4.9 4.5 1.0 N D:GLY13 4.9 2.8 1.0 OG1 D:THR14 4.9 4.3 1.0 CA D:GLY13 4.9 3.5 1.0 O D:PHE11 5.0 3.6 1.0

H.Rodriguez, I.Angulo, B.De Las Rivas, N.Campillo, J.A.Paez, R.Munoz, J.M.Mancheno. P-Coumaric Acid Decarboxylase From Lactobacillus Plantarum: Structural Insights Into the Active Site and Decarboxylation Catalytic Mechanism. Proteins V. 78 1662 2010.
ISSN: ISSN 0887-3585
PubMed: 20112419
DOI: 10.1002/PROT.22684