Zinc in PDB 3gzu: VP7 Recoated Rotavirus Dlp

The binding sites of Zinc atom in the VP7 Recoated Rotavirus Dlp (pdb code 3gzu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the VP7 Recoated Rotavirus Dlp, PDB code: 3gzu:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in the VP7 Recoated Rotavirus Dlp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of VP7 Recoated Rotavirus Dlp within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn398 b:42.6 occ:1.00 NE2 C:HIS153 2.5 88.6 1.0 NE2 D:HIS153 2.6 0.5 1.0 NE2 E:HIS153 2.8 92.1 1.0 CE1 C:HIS153 2.9 88.6 1.0 CE1 D:HIS153 3.2 0.5 1.0 CE1 E:HIS153 3.4 92.1 1.0 CD D:LYS154 3.5 73.5 1.0 CD2 D:HIS153 3.7 0.5 1.0 CD2 C:HIS153 3.8 88.6 1.0 CD C:LYS154 3.9 82.4 1.0 CD2 E:HIS153 4.1 92.1 1.0 ND1 C:HIS153 4.2 88.6 1.0 CD E:LYS154 4.3 75.6 1.0 NZ D:LYS154 4.4 73.5 1.0 NZ C:LYS154 4.4 82.4 1.0 ND1 D:HIS153 4.4 0.5 1.0 CG D:LYS154 4.5 73.5 1.0 CE D:LYS154 4.6 73.5 1.0 ND1 E:HIS153 4.6 92.1 1.0 CG C:HIS153 4.7 88.6 1.0 CG D:HIS153 4.7 0.5 1.0 CE C:LYS154 4.7 82.4 1.0 CG C:LYS154 4.9 82.4 1.0

Zinc binding site 2 out of 5 in the VP7 Recoated Rotavirus Dlp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of VP7 Recoated Rotavirus Dlp within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn398 b:42.6 occ:1.00 CE G:LYS154 0.9 73.5 1.0 CD G:LYS154 1.2 73.5 1.0 NZ G:LYS154 1.6 73.5 1.0 CG G:LYS154 2.5 73.5 1.0 CB G:LYS154 3.5 73.5 1.0 OG G:SER186 4.4 0.3 1.0 OE1 F:GLU327 4.9 0.8 1.0 CA G:LYS154 4.9 0.8 1.0

Zinc binding site 3 out of 5 in the VP7 Recoated Rotavirus Dlp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of VP7 Recoated Rotavirus Dlp within 5.0Å range: probe atom residue distance (Å) B Occ J:Zn398 b:42.6 occ:1.00 CE1 J:HIS153 2.9 0.5 1.0 CD J:LYS154 2.9 73.5 1.0 NE2 J:HIS153 3.2 0.5 1.0 CD K:LYS154 3.4 75.6 1.0 NZ K:LYS154 3.5 75.6 1.0 CG J:LYS154 3.5 73.5 1.0 OE1 J:GLU327 3.7 0.9 1.0 NE2 K:HIS153 3.7 92.1 1.0 CE K:LYS154 4.0 75.6 1.0 ND1 J:HIS153 4.0 0.5 1.0 CE J:LYS154 4.2 73.5 1.0 NZ J:LYS154 4.4 73.5 1.0 CE1 K:HIS153 4.4 92.1 1.0 CD2 J:HIS153 4.4 0.5 1.0 CB K:ALA338 4.5 0.4 1.0 NE2 I:HIS153 4.5 88.6 1.0 CG K:LYS154 4.6 75.6 1.0 CD2 K:HIS153 4.6 92.1 1.0 CB J:LYS154 4.6 73.5 1.0 CG J:HIS153 4.9 0.5 1.0 CD J:GLU327 4.9 0.9 1.0 CE1 I:HIS153 4.9 88.6 1.0

Zinc binding site 4 out of 5 in the VP7 Recoated Rotavirus Dlp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of VP7 Recoated Rotavirus Dlp within 5.0Å range: probe atom residue distance (Å) B Occ N:Zn398 b:42.6 occ:1.00 NE2 N:HIS153 2.6 92.1 1.0 NE2 M:HIS153 2.6 0.5 1.0 CE1 M:HIS153 2.9 0.5 1.0 NE2 L:HIS153 3.1 88.6 1.0 CE1 N:HIS153 3.1 92.1 1.0 CD N:LYS154 3.5 75.6 1.0 CD M:LYS154 3.7 73.5 1.0 CD2 N:HIS153 3.7 92.1 1.0 CE1 L:HIS153 3.7 88.6 1.0 CD2 M:HIS153 3.9 0.5 1.0 ND1 M:HIS153 4.2 0.5 1.0 CD2 L:HIS153 4.3 88.6 1.0 ND1 N:HIS153 4.3 92.1 1.0 NZ N:LYS154 4.4 75.6 1.0 CG N:LYS154 4.4 75.6 1.0 CG M:LYS154 4.5 73.5 1.0 CE N:LYS154 4.5 75.6 1.0 CD L:LYS154 4.5 82.4 1.0 NZ L:LYS154 4.6 82.4 1.0 CG N:HIS153 4.7 92.1 1.0 CG M:HIS153 4.7 0.5 1.0 NZ M:LYS154 4.8 73.5 1.0 CE M:LYS154 4.9 73.5 1.0 CB N:LYS154 4.9 75.6 1.0 CB N:ALA338 5.0 0.4 1.0 ND1 L:HIS153 5.0 88.6 1.0

Zinc binding site 5 out of 5 in the VP7 Recoated Rotavirus Dlp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of VP7 Recoated Rotavirus Dlp within 5.0Å range: probe atom residue distance (Å) B Occ O:Zn398 b:42.6 occ:0.33 NE2 O:HIS153 3.0 0.6 1.0 CE1 O:HIS153 3.2 0.6 1.0 CD2 O:HIS153 3.5 0.6 1.0 ND1 O:HIS153 3.7 0.6 1.0 CG O:HIS153 3.9 0.6 1.0

J.Z.Chen, E.C.Settembre, S.T.Aoki, X.Zhang, A.R.Bellamy, P.R.Dormitzer, S.C.Harrison, N.Grigorieff. Molecular Interactions in Rotavirus Assembly and Uncoating Seen By High-Resolution Cryo-Em. Proc.Natl.Acad.Sci.Usa V. 106 10644 2009.
ISSN: ISSN 0027-8424
PubMed: 19487668
DOI: 10.1073/PNAS.0904024106