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Zinc in PDB 4ygj: Nabr--Interactions Between Hofmeister Anions and the Binding Pocket of A Protein

Enzymatic activity of Nabr--Interactions Between Hofmeister Anions and the Binding Pocket of A Protein

All present enzymatic activity of Nabr--Interactions Between Hofmeister Anions and the Binding Pocket of A Protein:
4.2.1.1;

Protein crystallography data

The structure of Nabr--Interactions Between Hofmeister Anions and the Binding Pocket of A Protein, PDB code: 4ygj was solved by J.M.Fox, K.Kang, W.Sherman, A.Heroux, G.M.Sastry, M.Baghbanzadeh, M.R.Lockett, G.M.Whitesides, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.299, 41.379, 72.460, 90.00, 104.64, 90.00
R / Rfree (%) 12.7 / 14.7

Other elements in 4ygj:

The structure of Nabr--Interactions Between Hofmeister Anions and the Binding Pocket of A Protein also contains other interesting chemical elements:

Bromine (Br) 10 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Nabr--Interactions Between Hofmeister Anions and the Binding Pocket of A Protein (pdb code 4ygj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Nabr--Interactions Between Hofmeister Anions and the Binding Pocket of A Protein, PDB code: 4ygj:

Zinc binding site 1 out of 1 in 4ygj

Go back to Zinc Binding Sites List in 4ygj
Zinc binding site 1 out of 1 in the Nabr--Interactions Between Hofmeister Anions and the Binding Pocket of A Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Nabr--Interactions Between Hofmeister Anions and the Binding Pocket of A Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:8.0
occ:1.00
 O A:HOH647 1.9 10.5 1.0
NE2 A:HIS94 2.0 8.2 1.0
ND1 A:HIS119 2.0 7.4 1.0
NE2 A:HIS96 2.0 7.8 1.0
BR A:BR302 2.6 11.5 0.3
CE1 A:HIS119 2.9 7.3 1.0
CD2 A:HIS94 3.0 7.7 1.0
CD2 A:HIS96 3.0 7.9 1.0
CE1 A:HIS94 3.0 8.0 1.0
CE1 A:HIS96 3.0 8.7 1.0
CG A:HIS119 3.1 7.2 1.0
CB A:HIS119 3.6 7.3 1.0
O A:HOH556 3.7 13.1 1.0
OG1 A:THR199 3.8 8.2 1.0
OE1 A:GLU106 4.0 8.1 1.0
NE2 A:HIS119 4.1 7.8 1.0
ND1 A:HIS94 4.1 8.5 1.0
CG A:HIS94 4.1 8.2 1.0
BR A:BR303 4.1 14.1 0.3
ND1 A:HIS96 4.2 9.4 1.0
CG A:HIS96 4.2 7.7 1.0
CD2 A:HIS119 4.2 7.9 1.0
O A:HOH585 4.2 16.6 1.0
CD A:GLU106 4.9 8.0 1.0

Reference:

J.M.Fox, K.Kang, W.Sherman, A.Heroux, M.Sastry, M.Baghbanzadeh, M.R.Lockett, G.M.Whitesides. Interactions Between Hofmeister Anions and the Binding Pocket of A Protein. J.Am.Chem.Soc. 2015.
ISSN: ESSN 1520-5126
PubMed: 25738615
DOI: 10.1021/JACS.5B00187
Page generated: Wed Dec 16 05:57:06 2020

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