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Zinc in PDB 2jzw: How the Hiv-1 Nucleocapsid Protein Binds and Destabilises the (-)Primer Binding Site During Reverse Transcription

Zinc Binding Sites:

The binding sites of Zinc atom in the How the Hiv-1 Nucleocapsid Protein Binds and Destabilises the (-)Primer Binding Site During Reverse Transcription (pdb code 2jzw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the How the Hiv-1 Nucleocapsid Protein Binds and Destabilises the (-)Primer Binding Site During Reverse Transcription, PDB code: 2jzw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2jzw

Go back to Zinc Binding Sites List in 2jzw
Zinc binding site 1 out of 2 in the How the Hiv-1 Nucleocapsid Protein Binds and Destabilises the (-)Primer Binding Site During Reverse Transcription


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of How the Hiv-1 Nucleocapsid Protein Binds and Destabilises the (-)Primer Binding Site During Reverse Transcription within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn56

b:0.0
occ:1.00
NE2 A:HIS23 2.0 0.0 1.0
SG A:CYS15 2.2 0.0 1.0
SG A:CYS28 2.2 0.0 1.0
SG A:CYS18 2.2 0.0 1.0
HB2 A:CYS28 2.6 0.0 1.0
CB A:CYS28 3.0 0.0 1.0
HB3 A:CYS15 3.0 0.0 1.0
CB A:CYS15 3.0 0.0 1.0
HB3 A:CYS18 3.1 0.0 1.0
CD2 A:HIS23 3.1 0.0 1.0
HB2 A:CYS15 3.1 0.0 1.0
CE1 A:HIS23 3.1 0.0 1.0
CB A:CYS18 3.2 0.0 1.0
HD2 A:HIS23 3.3 0.0 1.0
HE1 A:HIS23 3.4 0.0 1.0
HB3 A:ASN17 3.6 0.0 1.0
HB3 A:CYS28 3.7 0.0 1.0
H A:CYS18 3.7 0.0 1.0
N A:CYS18 3.9 0.0 1.0
HA A:CYS28 3.9 0.0 1.0
H A:GLY19 4.0 0.0 1.0
CA A:CYS18 4.0 0.0 1.0
HB2 A:CYS18 4.1 0.0 1.0
CA A:CYS28 4.1 0.0 1.0
HB2 A:LYS20 4.1 0.0 1.0
CG A:HIS23 4.3 0.0 1.0
ND1 A:HIS23 4.3 0.0 1.0
H A:LYS20 4.4 0.0 1.0
HA A:ALA25 4.4 0.0 1.0
C A:ASN17 4.5 0.0 1.0
CA A:CYS15 4.5 0.0 1.0
N A:GLY19 4.5 0.0 1.0
O A:LYS20 4.6 0.0 1.0
CB A:ASN17 4.6 0.0 1.0
C A:CYS18 4.6 0.0 1.0
H A:ASN17 4.7 0.0 1.0
HB2 A:ALA30 4.8 0.0 1.0
N A:LYS20 4.8 0.0 1.0
HA A:CYS15 4.9 0.0 1.0
H A:CYS28 4.9 0.0 1.0
N A:CYS28 4.9 0.0 1.0
CA A:ASN17 5.0 0.0 1.0
CB A:LYS20 5.0 0.0 1.0
HA A:CYS18 5.0 0.0 1.0

Zinc binding site 2 out of 2 in 2jzw

Go back to Zinc Binding Sites List in 2jzw
Zinc binding site 2 out of 2 in the How the Hiv-1 Nucleocapsid Protein Binds and Destabilises the (-)Primer Binding Site During Reverse Transcription


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of How the Hiv-1 Nucleocapsid Protein Binds and Destabilises the (-)Primer Binding Site During Reverse Transcription within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn57

b:0.0
occ:1.00
NE2 A:HIS44 2.1 0.0 1.0
SG A:CYS39 2.2 0.0 1.0
SG A:CYS36 2.3 0.0 1.0
SG A:CYS49 2.3 0.0 1.0
OE2 A:GLU51 2.5 0.0 1.0
HB2 A:CYS49 2.5 0.0 1.0
HB3 A:CYS39 2.9 0.0 1.0
CB A:CYS49 2.9 0.0 1.0
CD2 A:HIS44 3.1 0.0 1.0
HB3 A:CYS49 3.1 0.0 1.0
CB A:CYS39 3.1 0.0 1.0
CE1 A:HIS44 3.2 0.0 1.0
CB A:CYS36 3.2 0.0 1.0
HB2 A:CYS36 3.2 0.0 1.0
HB3 A:CYS36 3.2 0.0 1.0
HD2 A:HIS44 3.3 0.0 1.0
HE1 A:HIS44 3.4 0.0 1.0
CD A:GLU51 3.5 0.0 1.0
H A:CYS39 3.6 0.0 1.0
HB2 A:LYS41 3.6 0.0 1.0
HB2 A:CYS39 3.9 0.0 1.0
H A:GLY40 4.1 0.0 1.0
OE1 A:GLU51 4.2 0.0 1.0
CA A:CYS39 4.2 0.0 1.0
HG3 A:GLU51 4.2 0.0 1.0
HD2 A:LYS41 4.2 0.0 1.0
N A:CYS39 4.2 0.0 1.0
CA A:CYS49 4.3 0.0 1.0
CG A:HIS44 4.3 0.0 1.0
HA A:MET46 4.3 0.0 1.0
ND1 A:HIS44 4.3 0.0 1.0
HA A:CYS49 4.4 0.0 1.0
H A:LYS41 4.4 0.0 1.0
HB2 A:GLU51 4.4 0.0 1.0
CG A:GLU51 4.4 0.0 1.0
O A:GLN45 4.6 0.0 1.0
HE22 A:GLN53 4.6 0.0 1.0
CB A:LYS41 4.6 0.0 1.0
CA A:CYS36 4.7 0.0 1.0
N A:GLY40 4.7 0.0 1.0
HB3 A:LYS38 4.7 0.0 1.0
O A:LYS41 4.8 0.0 1.0
H A:GLU51 4.8 0.0 1.0
C A:CYS39 4.8 0.0 1.0
H A:CYS49 4.8 0.0 1.0
N A:LYS41 4.9 0.0 1.0
HA A:CYS36 5.0 0.0 1.0

Reference:

S.Bourbigot, N.Ramalanjaona, C.Boudier, G.F.Salgado, B.P.Roques, Y.Mely, S.Bouaziz, N.Morellet. How the Hiv-1 Nucleocapsid Protein Binds and Destabilises the (-)Primer Binding Site During Reverse Transcription. J.Mol.Biol. V. 383 1112 2008.
ISSN: ISSN 0022-2836
PubMed: 18773912
DOI: 10.1016/J.JMB.2008.08.046
Page generated: Wed Dec 16 03:33:10 2020

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