Barium in PDB 3wjb: Crystal Structure of Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana

The structure of Crystal Structure of Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana, PDB code: 3wjb was solved by E.Mizohata, K.Fukumoto, A.Onoda, M.Bocola, M.Arlt, T.Inoue, U.Schwaneberg, T.Hayashi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.20
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	67.803, 67.803, 130.190, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 24.8

The binding sites of Barium atom in the Crystal Structure of Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana (pdb code 3wjb). This binding sites where shown within 5.0 Angstroms radius around Barium atom.
In total 4 binding sites of Barium where determined in the Crystal Structure of Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana, PDB code: 3wjb:
Jump to Barium binding site number: 1; 2; 3; 4;

Barium binding site 1 out of 4 in the Crystal Structure of Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana


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 Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba501 b:86.9 occ:0.50 O A:HOH616 2.2 20.6 1.0 O A:HOH647 2.7 22.3 1.0 O A:HOH634 2.9 30.3 1.0 O A:PRO86 3.0 27.0 1.0 O A:HOH615 3.8 37.5 1.0 C A:PRO86 4.2 28.2 1.0

Barium binding site 2 out of 4 in the Crystal Structure of Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana


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 Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba502 b:55.5 occ:1.00 O A:HOH673 2.4 46.1 1.0 O A:LEU137 2.6 39.3 1.0 O A:GLU112 2.9 39.3 1.0 OE2 A:GLU136 3.1 45.2 1.0 C A:GLU112 3.7 38.0 1.0 C A:LEU137 3.9 39.2 1.0 CD A:GLU136 4.0 41.0 1.0 CG A:GLU136 4.0 34.9 1.0 CA A:GLU112 4.1 40.1 1.0 CB A:GLN113 4.5 32.2 1.0 CG A:GLU112 4.5 46.2 1.0 CA A:VAL138 4.7 40.2 1.0 N A:VAL138 4.7 39.8 1.0 O A:ASP111 4.7 41.4 1.0 N A:GLN113 4.7 35.2 1.0 N A:LEU137 4.8 37.8 1.0 CA A:LEU137 4.9 39.2 1.0 CB A:GLU112 4.9 41.5 1.0

Barium binding site 3 out of 4 in the Crystal Structure of Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 3 of Crystal Structure of Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana within 5.0Å range: probe atom residue distance (Å) B Occ B:Ba501 b:93.8 occ:0.50 O B:PRO86 3.4 40.0 1.0 O B:HOH631 3.7 33.3 1.0 O B:HOH616 3.7 27.6 1.0 O B:HOH615 3.9 29.2 1.0 C B:PRO86 4.4 39.0 1.0

Barium binding site 4 out of 4 in the Crystal Structure of Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 4 of Crystal Structure of Mutant Nitrobindin M75L/H76L/Q96C/M148L/H158L (NB4) From Arabidopsis Thaliana within 5.0Å range: probe atom residue distance (Å) B Occ B:Ba502 b:44.6 occ:1.00 O B:HOH625 2.4 41.5 1.0 OE2 B:GLU136 2.8 31.0 1.0 O B:LEU137 2.9 40.3 1.0 O B:GLU112 2.9 29.7 1.0 CD B:GLU136 3.7 34.6 1.0 C B:LEU137 3.9 38.7 1.0 C B:GLU112 3.9 32.5 1.0 CG B:GLU136 4.1 37.0 1.0 CA B:GLU112 4.2 34.2 1.0 CA B:VAL138 4.3 38.9 1.0 N B:VAL138 4.4 38.6 1.0 CB B:VAL138 4.5 39.2 1.0 CB B:GLU112 4.5 34.3 1.0 OE1 B:GLU136 4.6 33.8 1.0 CG1 B:VAL138 4.9 36.4 1.0

K.Fukumoto, A.Onoda, E.Mizohata, M.Bocola, T.Inoue, U.Schwaneberg, T.Hayashi. A Rhodium Complex-Linked Hybrid Biocatalyst: Stereo-Controlled Phenylacetylene Polymerization Within An Engineered Protein Cavity Chemcatchem 2014.
ISSN: ESSN 1867-3899
DOI: 10.1002/CCTC.201301055