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Zinc in PDB 2ihx: Solution Structure of the Rous Sarcoma Virus Nucleocapsid Protein:Upsi Rna Packaging Signal Complex

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of the Rous Sarcoma Virus Nucleocapsid Protein:Upsi Rna Packaging Signal Complex (pdb code 2ihx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of the Rous Sarcoma Virus Nucleocapsid Protein:Upsi Rna Packaging Signal Complex, PDB code: 2ihx:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2ihx

Go back to Zinc Binding Sites List in 2ihx
Zinc binding site 1 out of 2 in the Solution Structure of the Rous Sarcoma Virus Nucleocapsid Protein:Upsi Rna Packaging Signal Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of the Rous Sarcoma Virus Nucleocapsid Protein:Upsi Rna Packaging Signal Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn235

b:63.4
occ:1.00
NE2 A:HIS29 2.0 41.2 1.0
SG A:CYS34 2.3 71.1 1.0
SG A:CYS24 2.3 41.1 1.0
SG A:CYS21 2.3 42.2 1.0
HD2 A:PRO35 2.6 61.3 1.0
HA A:CYS34 2.8 25.0 1.0
CD2 A:HIS29 2.9 24.5 1.0
HB2 A:CYS34 3.0 11.1 1.0
HD2 A:HIS29 3.0 44.0 1.0
CB A:CYS34 3.1 42.3 1.0
CE1 A:HIS29 3.1 1.2 1.0
HB3 A:CYS21 3.1 14.3 1.0
CB A:CYS21 3.1 43.2 1.0
H A:CYS24 3.2 53.5 1.0
HB2 A:CYS21 3.3 51.0 1.0
HB3 A:CYS24 3.4 73.2 1.0
HE1 A:HIS29 3.4 22.4 1.0
CA A:CYS34 3.5 4.3 1.0
CB A:CYS24 3.5 64.1 1.0
HB A:THR23 3.5 53.4 1.0
CD A:PRO35 3.7 12.1 1.0
H A:GLY25 3.9 15.1 1.0
N A:CYS24 3.9 71.2 1.0
HD3 A:PRO35 4.0 73.4 1.0
H A:SER26 4.0 74.2 1.0
CG A:HIS29 4.1 30.1 1.0
HB3 A:CYS34 4.1 2.2 1.0
ND1 A:HIS29 4.1 74.5 1.0
HB2 A:SER26 4.2 75.4 1.0
CA A:CYS24 4.3 3.5 1.0
H A:LYS36 4.3 2.2 1.0
HB2 A:CYS24 4.4 45.2 1.0
HA A:GLN31 4.4 54.3 1.0
N A:PRO35 4.4 33.4 1.0
C A:CYS34 4.4 11.3 1.0
O A:TYR30 4.5 60.0 1.0
HG2 A:PRO35 4.5 23.3 1.0
H A:THR23 4.5 24.4 1.0
N A:CYS34 4.5 54.5 1.0
CB A:THR23 4.6 70.2 1.0
CA A:CYS21 4.6 2.4 1.0
CG A:PRO35 4.7 31.3 1.0
N A:GLY25 4.7 13.1 1.0
HG22 A:THR23 4.7 3.5 1.0
O A:SER26 4.7 10.1 1.0
C A:TYR30 4.8 32.2 1.0
C A:THR23 4.8 51.2 1.0
N A:SER26 4.9 63.4 1.0
HA A:CYS21 4.9 24.3 1.0
HB3 A:LYS36 5.0 73.4 1.0
N A:THR23 5.0 11.4 1.0

Zinc binding site 2 out of 2 in 2ihx

Go back to Zinc Binding Sites List in 2ihx
Zinc binding site 2 out of 2 in the Solution Structure of the Rous Sarcoma Virus Nucleocapsid Protein:Upsi Rna Packaging Signal Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of the Rous Sarcoma Virus Nucleocapsid Protein:Upsi Rna Packaging Signal Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn236

b:52.1
occ:1.00
NE2 A:HIS55 2.0 75.4 1.0
SG A:CYS60 2.3 72.2 1.0
SG A:CYS50 2.3 0.4 1.0
SG A:CYS47 2.3 42.4 1.0
HB2 A:CYS60 2.8 43.0 1.0
CD2 A:HIS55 2.9 63.2 1.0
CE1 A:HIS55 3.0 73.4 1.0
CB A:CYS60 3.1 30.2 1.0
CB A:CYS47 3.1 10.1 1.0
HD2 A:HIS55 3.1 55.1 1.0
HB3 A:CYS47 3.1 0.2 1.0
HB2 A:CYS47 3.2 5.1 1.0
HE1 A:HIS55 3.3 51.5 1.0
HB3 A:CYS50 3.4 33.0 1.0
H A:CYS50 3.4 13.4 1.0
CB A:CYS50 3.5 23.4 1.0
HA3 A:GLY52 3.6 52.3 1.0
H A:GLY52 3.6 4.4 1.0
HB3 A:CYS60 3.8 13.2 1.0
HA A:CYS60 3.9 51.4 1.0
H2' B:A197 4.0 20.1 1.0
N A:CYS50 4.0 53.2 1.0
CG A:HIS55 4.1 31.5 1.0
ND1 A:HIS55 4.1 62.1 1.0
CA A:CYS60 4.1 12.2 1.0
H8 B:A197 4.2 2.3 1.0
C8 B:A197 4.2 65.4 1.0
HA A:ALA57 4.2 52.1 1.0
CA A:CYS50 4.2 12.4 1.0
N7 B:A197 4.3 74.4 1.0
HB3 A:LEU49 4.3 41.4 1.0
HB2 A:CYS50 4.4 22.3 1.0
N A:GLY52 4.4 31.2 1.0
CA A:GLY52 4.5 60.3 1.0
H A:LEU49 4.5 45.3 1.0
CA A:CYS47 4.6 5.5 1.0
HB2 A:LEU49 4.6 41.4 1.0
C A:CYS50 4.7 0.0 1.0
N9 B:A197 4.9 44.5 1.0
HA A:CYS47 4.9 50.3 1.0
CB A:LEU49 4.9 22.4 1.0
C5 B:A197 4.9 63.4 1.0
H A:ARG61 5.0 53.1 1.0
C A:LEU49 5.0 50.1 1.0
O A:ASN56 5.0 5.2 1.0

Reference:

J.Zhou, R.L.Bean, V.M.Vogt, M.Summers. Solution Structure of the Rous Sarcoma Virus Nucleocapsid Protein: Mupsi Rna Packaging Signal Complex. J.Mol.Biol. V. 365 453 2007.
ISSN: ISSN 0022-2836
PubMed: 17070546
DOI: 10.1016/J.JMB.2006.10.013
Page generated: Thu Oct 17 00:54:43 2024

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