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Chlorine in PDB 4hjj: Structure Reveals Function of the Dual Variable Domain Immunoglobulin (Dvd-Ig) Molecule

Protein crystallography data

The structure of Structure Reveals Function of the Dual Variable Domain Immunoglobulin (Dvd-Ig) Molecule, PDB code: 4hjj was solved by C.G.Jakob, R.Edalji, R.A.Judge, E.Digiammarino, Y.Li, J.Gu, T.Ghayur, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.17 / 2.10
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 274.385, 65.498, 78.802, 90.00, 95.20, 90.00
R / Rfree (%) 18.4 / 22

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure Reveals Function of the Dual Variable Domain Immunoglobulin (Dvd-Ig) Molecule (pdb code 4hjj). 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 Structure Reveals Function of the Dual Variable Domain Immunoglobulin (Dvd-Ig) Molecule, PDB code: 4hjj:

Chlorine binding site 1 out of 1 in 4hjj

Go back to Chlorine Binding Sites List in 4hjj
Chlorine binding site 1 out of 1 in the Structure Reveals Function of the Dual Variable Domain Immunoglobulin (Dvd-Ig) Molecule


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure Reveals Function of the Dual Variable Domain Immunoglobulin (Dvd-Ig) Molecule within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Cl402

b:74.3
occ:1.00
NZ L:LYS45 3.0 63.8 1.0
O L:HOH509 3.8 36.7 1.0
NE2 L:GLN42 3.8 49.1 1.0
NZ L:LYS39 3.9 48.2 1.0
CE L:LYS45 4.0 60.6 1.0
O L:HOH630 4.1 59.7 1.0
CD L:LYS45 4.2 49.7 1.0
CD L:LYS39 4.2 43.7 1.0
CE L:LYS39 4.3 47.5 1.0
OE1 L:GLN42 4.3 61.3 1.0
CD L:GLN42 4.5 63.3 1.0
OE1 L:GLN37 4.6 38.3 1.0
O L:HOH650 4.8 73.4 1.0

Reference:

C.G.Jakob, R.Edalji, R.A.Judge, E.Digiammarino, Y.Li, J.Gu, T.Ghayur. Structure Reveals Function of the Dual Variable Domain Immunoglobulin (Dvd-Ig[Tm]) Molecule Mabs V. 5 358 2013.
ISSN: ISSN 1942-0862
PubMed: 23549062
DOI: 10.4161/MABS.23977
Page generated: Sat Dec 12 10:42:58 2020

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