Zinc in PDB 6fbr: Crystal Structure of the Human Retinoid X Receptor Dna-Binding Domain Bound to the Human Mep DR1 Response Element, pH 4.2

Protein crystallography data

The structure of Crystal Structure of the Human Retinoid X Receptor Dna-Binding Domain Bound to the Human Mep DR1 Response Element, pH 4.2, PDB code: 6fbr was solved by A.G.Mcewen, P.Poussin-Courmontagne, J.Osz, N.Rochel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.29 / 2.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 55.659, 55.659, 166.131, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 23.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Human Retinoid X Receptor Dna-Binding Domain Bound to the Human Mep DR1 Response Element, pH 4.2 (pdb code 6fbr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Human Retinoid X Receptor Dna-Binding Domain Bound to the Human Mep DR1 Response Element, pH 4.2, PDB code: 6fbr:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6fbr

Go back to Zinc Binding Sites List in 6fbr
Zinc binding site 1 out of 2 in the Crystal Structure of the Human Retinoid X Receptor Dna-Binding Domain Bound to the Human Mep DR1 Response Element, pH 4.2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Human Retinoid X Receptor Dna-Binding Domain Bound to the Human Mep DR1 Response Element, pH 4.2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:54.0
occ:1.00
SG A:CYS152 2.3 40.8 1.0
SG A:CYS155 2.3 45.7 1.0
SG A:CYS135 2.4 44.7 1.0
SG A:CYS138 2.4 42.9 1.0
CB A:CYS135 3.3 41.8 1.0
CB A:CYS155 3.3 40.7 1.0
CB A:CYS138 3.4 40.3 1.0
CB A:CYS152 3.5 37.8 1.0
N A:CYS138 3.8 41.8 1.0
N A:CYS152 3.9 37.8 1.0
N A:CYS155 4.1 39.9 1.0
NH1 A:ARG184 4.2 42.5 1.0
CA A:CYS138 4.2 41.7 1.0
CA A:CYS152 4.3 37.9 1.0
CA A:CYS155 4.3 39.8 1.0
CB A:ILE137 4.4 45.0 1.0
CB A:ASP140 4.4 35.8 1.0
NH2 A:ARG191 4.7 32.7 1.0
CA A:CYS135 4.7 43.8 1.0
C A:CYS138 4.8 45.0 1.0
C A:ILE137 4.8 45.7 1.0
N A:ASP140 4.9 37.3 1.0
N A:GLY139 4.9 40.5 1.0
C A:CYS152 4.9 41.6 1.0
CD A:ARG184 4.9 42.5 1.0
CA A:ILE137 5.0 43.3 1.0
O A:CYS152 5.0 40.1 1.0

Zinc binding site 2 out of 2 in 6fbr

Go back to Zinc Binding Sites List in 6fbr
Zinc binding site 2 out of 2 in the Crystal Structure of the Human Retinoid X Receptor Dna-Binding Domain Bound to the Human Mep DR1 Response Element, pH 4.2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Human Retinoid X Receptor Dna-Binding Domain Bound to the Human Mep DR1 Response Element, pH 4.2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:56.0
occ:1.00
SG B:CYS138 2.3 47.1 1.0
SG B:CYS135 2.3 43.0 1.0
SG B:CYS155 2.4 44.4 1.0
SG B:CYS152 2.4 45.5 1.0
CB B:CYS135 3.2 39.6 1.0
CB B:CYS155 3.3 39.3 1.0
CB B:CYS138 3.4 44.0 1.0
CB B:CYS152 3.6 41.8 1.0
N B:CYS138 3.7 45.0 1.0
N B:CYS152 3.9 41.2 1.0
CA B:CYS138 4.1 44.9 1.0
N B:CYS155 4.1 39.9 1.0
CB B:ILE137 4.3 47.7 1.0
CA B:CYS155 4.3 39.4 1.0
CA B:CYS152 4.3 40.8 1.0
NH1 B:ARG184 4.5 46.7 1.0
CB B:ASP140 4.5 45.0 1.0
CA B:CYS135 4.6 41.0 1.0
C B:ILE137 4.7 50.1 1.0
C B:CYS138 4.8 51.5 1.0
NH2 B:ARG191 4.9 42.8 1.0
N B:GLY139 4.9 48.4 1.0
N B:ASP140 4.9 44.7 1.0
CD B:ARG184 4.9 48.1 1.0
CA B:ILE137 4.9 45.1 1.0
CG1 B:ILE137 4.9 48.9 1.0

Reference:

J.Osz, A.G.Mcewen, J.Wolf, P.Poussin-Courmontagne, C.Peluso-Iltis, Y.Chebaro, B.Kieffer, N.Rochel. Modulation of Rxr-Dna Complex Assembly By Dna Context. Mol. Cell. Endocrinol. V. 481 44 2019.
ISSN: ISSN 1872-8057
PubMed: 30476562
DOI: 10.1016/J.MCE.2018.11.008
Page generated: Wed Dec 16 11:47:04 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy