Zinc in PDB 4cs9: Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate

The structure of Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate, PDB code: 4cs9 was solved by C.Leyrat, M.Renner, K.Harlos, J.M.Grimes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.80 / 2.01
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.050, 93.610, 85.600, 90.00, 95.76, 90.00
R / Rfree (%)	18.64 / 20.83

The binding sites of Zinc atom in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate (pdb code 4cs9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate, PDB code: 4cs9:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate


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 Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1171 b:39.3 occ:0.83 NE2 A:HIS25 2.0 47.4 1.0 SG A:CYS15 2.1 42.0 1.0 SG A:CYS21 2.3 54.7 1.0 SG A:CYS7 2.3 39.1 1.0 CE1 A:HIS25 2.8 47.8 1.0 CD2 A:HIS25 3.1 47.5 1.0 CB A:CYS15 3.1 40.2 1.0 CB A:CYS7 3.2 35.4 1.0 CB A:CYS21 3.3 53.5 1.0 ND1 A:HIS25 4.0 48.5 1.0 CG A:HIS25 4.2 45.8 1.0 O A:HOH2021 4.4 61.3 1.0 CA A:CYS15 4.6 41.8 1.0 CA A:CYS7 4.6 35.9 1.0 C2 A:AMP1172 4.6 60.2 1.0 CD2 A:TYR9 4.7 36.3 1.0 CA A:CYS21 4.7 55.5 1.0 O A:HOH2013 4.8 68.0 1.0 O A:PHE23 4.8 47.0 1.0 CB A:TYR9 4.9 32.9 1.0 CB A:PHE23 4.9 47.3 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate


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 Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1170 b:38.2 occ:0.83 NE2 B:HIS25 2.0 46.6 1.0 SG B:CYS15 2.2 46.5 1.0 SG B:CYS21 2.3 51.1 1.0 SG B:CYS7 2.3 44.8 1.0 CE1 B:HIS25 3.0 46.9 1.0 CB B:CYS15 3.1 42.5 1.0 CD2 B:HIS25 3.1 46.2 1.0 CB B:CYS21 3.2 48.3 1.0 CB B:CYS7 3.3 41.5 1.0 O B:HOH2012 4.1 43.8 1.0 ND1 B:HIS25 4.2 47.4 1.0 CG B:HIS25 4.2 44.6 1.0 NE B:ARG17 4.4 81.8 1.0 CA B:CYS15 4.5 42.3 1.0 CA B:CYS21 4.6 49.4 1.0 CA B:CYS7 4.6 41.7 1.0 CD2 B:TYR9 4.6 42.5 1.0 CB B:TYR9 4.8 39.7 1.0 CB B:PHE23 4.8 49.5 1.0 NH2 B:ARG17 4.9 66.0 1.0 C B:CYS21 4.9 52.8 1.0 N B:PHE23 5.0 49.3 1.0 O B:PHE23 5.0 49.0 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1173 b:37.5 occ:0.82 NE2 C:HIS25 1.9 40.9 1.0 SG C:CYS15 2.2 48.9 1.0 SG C:CYS7 2.3 40.6 1.0 SG C:CYS21 2.4 47.4 1.0 CE1 C:HIS25 2.9 41.7 1.0 CD2 C:HIS25 3.0 40.7 1.0 CB C:CYS15 3.0 44.6 1.0 CB C:CYS21 3.1 44.8 1.0 CB C:CYS7 3.2 36.5 1.0 O C:HOH2015 3.9 49.8 1.0 ND1 C:HIS25 4.0 42.4 1.0 CG C:HIS25 4.1 40.1 1.0 N6 C:AMP1174 4.4 46.1 0.7 CA C:CYS15 4.5 44.5 1.0 O C:HOH2019 4.5 54.3 1.0 CA C:CYS7 4.6 36.0 1.0 CA C:CYS21 4.6 46.1 1.0 CB C:PHE23 4.9 45.1 1.0 CD2 C:TYR9 5.0 47.4 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to Adenosine Monophosphate within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn1178 b:31.6 occ:0.94 NE2 E:HIS25 2.0 38.6 1.0 SG E:CYS15 2.2 35.6 1.0 SG E:CYS7 2.3 37.5 1.0 SG E:CYS21 2.4 34.4 1.0 CE1 E:HIS25 3.0 38.4 1.0 CD2 E:HIS25 3.1 38.1 1.0 CB E:CYS15 3.1 32.3 1.0 CB E:CYS21 3.3 32.0 1.0 CB E:CYS7 3.3 34.4 1.0 O E:HOH2018 3.9 34.9 1.0 ND1 E:HIS25 4.1 38.8 1.0 O E:HOH2004 4.1 54.5 1.0 CG E:HIS25 4.2 37.3 1.0 CA E:CYS15 4.4 33.4 1.0 CA E:CYS7 4.6 35.0 1.0 CD2 E:TYR9 4.7 38.0 1.0 CA E:CYS21 4.7 33.0 1.0 CB E:PHE23 4.8 39.3 1.0 CB E:ARG17 4.8 35.3 1.0 CB E:TYR9 4.9 35.6 1.0

C.Leyrat, M.Renner, K.Harlos, J.T.Huiskonen, J.M.Grimes. Drastic Changes in Conformational Dynamics of the Antiterminator M2-1 Regulate Transcription Efficiency in Pneumovirinae. Elife V. 3 02674 2014.
ISSN: ISSN 2050-084X
PubMed: 24842877
DOI: 10.7554/ELIFE.02674