Chlorine in PDB 5bjz: Crystal Structure of Maltose Binding Protein in Complex with An Allosteric Synthetic Antibody

The structure of Crystal Structure of Maltose Binding Protein in Complex with An Allosteric Synthetic Antibody, PDB code: 5bjz was solved by S.Mukherjee, A.A.Kossiakoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	98.390, 87.590, 114.650, 90.00, 114.29, 90.00
R / Rfree (%)	19.4 / 22.9

The binding sites of Chlorine atom in the Crystal Structure of Maltose Binding Protein in Complex with An Allosteric Synthetic Antibody (pdb code 5bjz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Maltose Binding Protein in Complex with An Allosteric Synthetic Antibody, PDB code: 5bjz:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Maltose Binding Protein in Complex with An Allosteric Synthetic Antibody


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Maltose Binding Protein in Complex with An Allosteric Synthetic Antibody within 5.0Å range: probe atom residue distance (Å) B Occ L:Cl301 b:68.0 occ:1.00 CA L:GLY69 3.4 34.1 1.0 CB A:PRO315 3.5 38.0 1.0 CA A:PRO315 3.6 37.0 1.0 CB A:ALA318 3.6 29.9 1.0 C L:GLY69 3.7 31.5 1.0 NH1 L:ARG67 4.1 35.1 1.0 O L:GLY69 4.1 33.4 1.0 N L:THR70 4.1 32.3 1.0 CG2 L:THR70 4.4 43.7 1.0 N A:PRO315 4.5 38.8 1.0 O A:PRO315 4.5 33.1 1.0 C A:PRO315 4.6 35.2 1.0 N L:GLY69 4.7 36.5 1.0 O A:ALA312 4.8 34.3 1.0 CG A:PRO315 4.8 40.1 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Maltose Binding Protein in Complex with An Allosteric Synthetic Antibody


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Maltose Binding Protein in Complex with An Allosteric Synthetic Antibody within 5.0Å range: probe atom residue distance (Å) B Occ H:Cl302 b:74.4 occ:1.00 O H:HOH470 2.8 50.4 1.0 O H:ARG144 3.2 46.1 1.0 CG H:ARG144 3.5 59.3 1.0 NE H:ARG144 3.6 70.4 1.0 CG2 H:VAL165 3.9 38.8 1.0 C H:ARG144 4.1 45.8 1.0 CD H:ARG144 4.1 64.8 1.0 CZ H:ARG144 4.4 73.0 1.0 CD1 H:LEU177 4.5 41.8 1.0 NH2 H:ARG144 4.6 74.6 1.0 CB H:ARG144 4.6 52.1 1.0 CA H:GLU145 4.7 49.6 1.0 N H:ALA146 4.7 55.4 1.0 OE1 H:GLU163 4.8 77.5 1.0 N H:GLU145 4.8 44.8 1.0 CG1 H:VAL165 4.9 33.3 1.0 CA H:ARG144 4.9 46.6 1.0 CB H:VAL165 4.9 35.7 1.0

S.Mukherjee, D.H.Griffin, J.R.Horn, S.S.Rizk, M.Nocula-Lugowska, M.Malmqvist, S.S.Kim, A.A.Kossiakoff. Engineered Synthetic Antibodies As Probes to Quantify the Energetic Contributions of Ligand Binding to Conformational Changes in Proteins. J. Biol. Chem. V. 293 2815 2018.
ISSN: ESSN 1083-351X
PubMed: 29321208
DOI: 10.1074/JBC.RA117.000656