Zinc in PDB 6g0y: X-Ray Structure of M-21 Protein Complex

The structure of X-Ray Structure of M-21 Protein Complex, PDB code: 6g0y was solved by T.A.Edwards, J.Barr, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.35 / 2.42
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	96.555, 116.524, 72.630, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 28

The binding sites of Zinc atom in the X-Ray Structure of M-21 Protein Complex (pdb code 6g0y). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the X-Ray Structure of M-21 Protein Complex, PDB code: 6g0y:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the X-Ray Structure of M-21 Protein Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Structure of M-21 Protein Complex within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn201 b:47.7 occ:1.00 NE2 F:HIS25 2.1 47.6 1.0 SG F:CYS7 2.2 44.0 1.0 SG F:CYS15 2.2 53.3 1.0 SG F:CYS21 2.3 61.9 1.0 CD2 F:HIS25 3.1 47.4 1.0 CE1 F:HIS25 3.1 47.0 1.0 CB F:CYS15 3.2 48.4 1.0 CB F:CYS7 3.2 38.9 1.0 CB F:CYS21 3.3 59.9 1.0 ND1 F:HIS25 4.2 46.1 1.0 CG F:HIS25 4.2 45.6 1.0 CA F:CYS15 4.5 43.8 1.0 CA F:CYS7 4.6 40.4 1.0 ND2 F:ASN17 4.6 58.4 1.0 CD1 F:PHE9 4.6 34.8 1.0 CB F:PHE23 4.8 51.7 1.0 CA F:CYS21 4.8 57.6 1.0 CB F:PHE9 4.9 35.2 1.0 O F:PHE23 4.9 39.3 1.0

Zinc binding site 2 out of 4 in the X-Ray Structure of M-21 Protein Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of X-Ray Structure of M-21 Protein Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:45.8 occ:1.00 NE2 A:HIS25 2.0 48.8 1.0 SG A:CYS21 2.1 50.3 1.0 SG A:CYS15 2.2 43.4 1.0 SG A:CYS7 2.2 48.2 1.0 CE1 A:HIS25 2.9 49.4 1.0 CB A:CYS15 3.0 41.2 1.0 CD2 A:HIS25 3.1 50.9 1.0 CB A:CYS21 3.2 59.8 1.0 CB A:CYS7 3.2 44.4 1.0 O A:HOH312 3.5 43.3 1.0 ND1 A:HIS25 4.0 43.9 1.0 CG A:HIS25 4.1 43.7 1.0 CA A:CYS15 4.4 41.1 1.0 CA A:CYS7 4.6 42.9 1.0 CB A:PHE23 4.6 57.7 1.0 CA A:CYS21 4.6 58.6 1.0 CD1 A:PHE9 4.9 42.2 1.0 CB A:PHE9 4.9 41.1 1.0 ND2 A:ASN17 5.0 58.9 1.0

Zinc binding site 3 out of 4 in the X-Ray Structure of M-21 Protein Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of X-Ray Structure of M-21 Protein Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn201 b:45.4 occ:1.00 SG C:CYS7 2.0 44.4 1.0 NE2 C:HIS25 2.1 39.1 1.0 SG C:CYS21 2.2 45.3 1.0 SG C:CYS15 2.2 36.1 1.0 CE1 C:HIS25 3.0 40.6 1.0 CB C:CYS15 3.1 38.2 1.0 CD2 C:HIS25 3.2 34.9 1.0 CB C:CYS21 3.2 50.2 1.0 CB C:CYS7 3.5 42.7 1.0 ND1 C:HIS25 4.1 39.4 1.0 CG C:HIS25 4.3 36.0 1.0 CA C:CYS15 4.5 40.0 1.0 CB C:PHE9 4.5 38.6 1.0 CA C:CYS7 4.5 47.0 1.0 CA C:CYS21 4.6 55.9 1.0 ND2 C:ASN17 4.8 55.7 1.0 CD1 C:PHE9 4.9 38.8 1.0 CB C:PHE23 4.9 42.4 1.0

Zinc binding site 4 out of 4 in the X-Ray Structure of M-21 Protein Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of X-Ray Structure of M-21 Protein Complex within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn201 b:42.4 occ:1.00 NE2 E:HIS25 1.9 43.3 1.0 SG E:CYS7 2.1 33.0 1.0 SG E:CYS15 2.3 40.8 1.0 SG E:CYS21 2.4 44.9 1.0 CE1 E:HIS25 2.8 46.3 1.0 CD2 E:HIS25 3.1 45.2 1.0 CB E:CYS15 3.1 34.0 1.0 CB E:CYS7 3.2 38.2 1.0 CB E:CYS21 3.3 52.7 1.0 ND1 E:HIS25 3.9 45.4 1.0 CG E:HIS25 4.1 43.5 1.0 CA E:CYS7 4.5 39.8 1.0 CA E:CYS15 4.5 35.7 1.0 ND2 E:ASN17 4.7 63.4 1.0 CA E:CYS21 4.8 56.5 1.0 CB E:PHE9 4.9 32.6 1.0 CD1 E:PHE9 4.9 33.5 1.0

M.Selvaraj, K.Yegambaram, E.J.A.A.Todd, C.A.Richard, R.L.Dods, G.M.Pangratiou, C.H.Trinh, S.L.Moul, J.C.Murphy, J.Mankouri, J.F.Eleouet, J.N.Barr, T.A.Edwards. The Structure of the Human Respiratory Syncytial Virus M2-1 Protein Bound to the Interaction Domain of the Phosphoprotein P Defines the Orientation of the Complex. Mbio V. 9 2018.
ISSN: ESSN 2150-7511
PubMed: 30425144
DOI: 10.1128/MBIO.01554-18