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Chlorine in PDB 5bk1: Crystal Structure of Maltose Binding Protein in Complex with An Endosteric Synthetic Antibody

Protein crystallography data

The structure of Crystal Structure of Maltose Binding Protein in Complex with An Endosteric Synthetic Antibody, PDB code: 5bk1 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) 19.81 / 2.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.830, 120.810, 193.600, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 25.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Maltose Binding Protein in Complex with An Endosteric Synthetic Antibody (pdb code 5bk1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Maltose Binding Protein in Complex with An Endosteric Synthetic Antibody, PDB code: 5bk1:

Chlorine binding site 1 out of 1 in 5bk1

Go back to Chlorine Binding Sites List in 5bk1
Chlorine binding site 1 out of 1 in the Crystal Structure of Maltose Binding Protein in Complex with An Endosteric 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 Endosteric Synthetic Antibody within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl301

b:61.5
occ:1.00
N C:TYR63 3.2 28.8 1.0
CE C:LYS68 3.3 50.3 1.0
NZ C:LYS68 3.7 48.1 1.0
CA C:SER62 3.7 34.5 1.0
O C:TYR63 3.9 30.9 1.0
C C:SER62 3.9 30.2 1.0
OG C:SER62 4.0 48.8 1.0
CD2 C:TYR63 4.1 30.2 1.0
CA C:TYR63 4.1 30.1 1.0
CB C:TYR63 4.1 30.6 1.0
O C:THR61 4.4 33.6 1.0
C C:TYR63 4.5 32.8 1.0
CB C:SER62 4.5 41.9 1.0
CG C:TYR63 4.6 30.7 1.0
CD C:LYS68 4.7 49.4 1.0
N C:SER62 4.8 31.4 1.0
C C:THR61 5.0 34.0 1.0

Reference:

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
Page generated: Sat Dec 12 11:32:12 2020

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