Atomistry » Zinc » PDB 2xy4-2y7f » 2y3g
Atomistry »
  Zinc »
    PDB 2xy4-2y7f »
      2y3g »

Zinc in PDB 2y3g: Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs

Protein crystallography data

The structure of Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs, PDB code: 2y3g was solved by J.Trepreau, E.Girard, A.P.Maillard, E.De Rosny, I.Petit-Haertlein, R.Kahn, J.Coves, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.666 / 1.91
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 31.896, 81.809, 93.336, 90.00, 90.47, 90.00
R / Rfree (%) 18.73 / 23.82

Other elements in 2y3g:

The structure of Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs (pdb code 2y3g). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs, PDB code: 2y3g:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 2y3g

Go back to Zinc Binding Sites List in 2y3g
Zinc binding site 1 out of 3 in the Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn150

b:40.7
occ:0.60
NE2 A:HIS46 2.0 69.1 0.6
OE1 A:GLU63 2.2 35.9 1.0
NE2 A:HIS42 2.3 71.0 1.0
NE2 A:HIS119 2.5 32.5 1.0
OE2 A:GLU63 2.5 40.8 1.0
CE1 A:HIS46 2.6 68.3 0.6
CD A:GLU63 2.7 45.9 1.0
CD2 A:HIS42 2.7 67.5 1.0
CD2 A:HIS46 3.1 65.9 0.6
CD2 A:HIS119 3.1 32.1 1.0
CE1 A:HIS42 3.5 73.2 1.0
CE1 A:HIS119 3.6 27.4 1.0
ND1 A:HIS46 3.7 65.3 0.6
SE A:MSE123 3.8 47.6 0.8
CG A:HIS46 4.0 65.7 0.6
CE A:MSE123 4.0 6.8 0.2
CG A:HIS42 4.0 67.1 1.0
CG A:GLU63 4.2 33.5 1.0
CD2 A:PHE66 4.2 29.1 1.0
CE A:MSE123 4.3 14.5 0.8
ND1 A:HIS42 4.4 69.9 1.0
CG A:HIS119 4.4 25.1 1.0
CE2 A:PHE66 4.6 37.8 1.0
ND1 A:HIS119 4.6 31.1 1.0
CB A:GLU63 4.9 28.0 1.0
CG A:MSE123 4.9 27.8 0.2
O A:HIS42 4.9 54.2 1.0
ND1 A:HIS46 5.0 68.0 0.4
CG A:MSE123 5.0 29.7 0.8

Zinc binding site 2 out of 3 in 2y3g

Go back to Zinc Binding Sites List in 2y3g
Zinc binding site 2 out of 3 in the Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn150

b:36.4
occ:0.40
OE2 B:GLU63 2.1 48.6 1.0
NE2 B:HIS42 2.1 67.5 1.0
NE2 B:HIS46 2.1 29.2 0.4
NE2 B:HIS119 2.3 29.1 1.0
CD2 B:HIS42 2.5 70.9 1.0
CD B:GLU63 2.7 55.0 1.0
OE1 B:GLU63 2.7 51.7 1.0
CD2 B:HIS46 2.8 32.3 0.4
CD2 B:HIS119 3.0 31.2 1.0
CE1 B:HIS46 3.3 34.6 0.4
CE1 B:HIS42 3.3 65.2 1.0
CE1 B:HIS119 3.5 31.8 1.0
SE B:MSE123 3.6 37.9 0.5
CG B:HIS42 3.8 66.3 1.0
SE B:MSE123 4.0 40.5 0.3
CE B:MSE123 4.0 21.1 0.5
CG B:HIS46 4.1 39.2 0.4
CG B:GLU63 4.1 51.4 1.0
ND1 B:HIS42 4.2 64.1 1.0
CD2 B:PHE66 4.2 30.9 1.0
CG B:HIS119 4.2 26.8 1.0
ND1 B:HIS46 4.3 33.1 0.4
CE B:MSE123 4.3 12.2 0.2
ND1 B:HIS119 4.4 25.7 1.0
CE2 B:PHE66 4.6 38.4 1.0
CG B:MSE123 4.8 24.9 0.2
SE B:MSE123 4.9 41.5 0.2
CG B:MSE123 4.9 25.0 0.3
CG B:MSE123 4.9 24.1 0.5

Zinc binding site 3 out of 3 in 2y3g

Go back to Zinc Binding Sites List in 2y3g
Zinc binding site 3 out of 3 in the Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn150

b:47.1
occ:0.25
OE1 C:GLU63 2.2 77.1 1.0
NE2 C:HIS42 2.4 58.6 1.0
NE2 C:HIS119 2.5 41.3 1.0
NE2 C:HIS46 2.5 70.4 0.6
SE C:MSE123 2.7 61.6 0.6
CD C:GLU63 2.8 80.2 1.0
CD2 C:HIS42 2.9 56.2 1.0
CD2 C:HIS119 3.2 35.2 1.0
CD2 C:HIS46 3.3 67.6 0.6
OE2 C:GLU63 3.3 86.5 1.0
CE1 C:HIS119 3.5 42.3 1.0
CE1 C:HIS46 3.5 73.2 0.6
CE1 C:HIS42 3.6 63.4 1.0
CG C:GLU63 3.6 72.9 1.0
CG C:MSE123 3.6 33.3 0.6
CG C:MSE123 3.7 25.9 0.4
CE C:MSE123 3.8 27.8 0.6
SE C:MSE123 4.0 48.0 0.4
CG C:HIS42 4.2 51.9 1.0
O C:HOH2009 4.4 46.8 1.0
CG C:HIS119 4.4 31.2 1.0
ND1 C:HIS42 4.5 59.8 1.0
CG C:HIS46 4.5 67.7 0.6
ND1 C:HIS119 4.5 29.9 1.0
ND1 C:HIS46 4.6 72.5 0.6
CB C:GLU63 4.7 62.4 1.0
CA C:GLU63 4.9 46.4 1.0
CB C:MSE123 4.9 30.6 0.4
CD2 C:PHE66 5.0 35.0 1.0

Reference:

J.Trepreau, E.Girard, A.P.Maillard, E.De Rosny, I.Petit-Haertlein, R.Kahn, J.Coves. Structural Basis For Metal Sensing By Cnrx. J.Mol.Biol. V. 408 766 2011.
ISSN: ISSN 0022-2836
PubMed: 21414325
DOI: 10.1016/J.JMB.2011.03.014
Page generated: Thu Oct 17 05:42:48 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy