Cadmium in PDB 4c3d: Hrsv M2-1, P422 Crystal Form

The structure of Hrsv M2-1, P422 Crystal Form, PDB code: 4c3d was solved by S.J.Tanner, A.Ariza, C.A.Richard, W.Wu, J.Trincao, J.A.Hiscox, M.W.Carroll, N.J.Silman, J.F.Eleouet, T.A.Edwards, J.N.Barr, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.74 / 2.52
Space group	P 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	102.275, 102.275, 90.993, 90.00, 90.00, 90.00
R / Rfree (%)	21.095 / 26.323

The binding sites of Cadmium atom in the Hrsv M2-1, P422 Crystal Form (pdb code 4c3d). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 4 binding sites of Cadmium where determined in the Hrsv M2-1, P422 Crystal Form, PDB code: 4c3d:
Jump to Cadmium binding site number: 1; 2; 3; 4;

Cadmium binding site 1 out of 4 in the Hrsv M2-1, P422 Crystal Form


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Hrsv M2-1, P422 Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd201 b:41.1 occ:1.00 NE2 A:HIS25 2.2 47.0 1.0 SG A:CYS15 2.3 41.8 1.0 SG A:CYS21 2.5 49.6 1.0 SG A:CYS7 2.6 40.9 1.0 CE1 A:HIS25 3.1 49.0 1.0 CB A:CYS15 3.3 45.0 1.0 CD2 A:HIS25 3.3 43.7 1.0 CB A:CYS7 3.3 39.4 1.0 CB A:CYS21 3.4 52.1 1.0 ND1 A:HIS25 4.3 40.4 1.0 CG A:HIS25 4.4 39.5 1.0 CA A:CYS15 4.6 40.4 1.0 CA A:CYS7 4.7 36.5 1.0 CB A:PHE23 4.7 46.0 1.0 CD2 A:PHE9 4.8 37.2 1.0 CB A:PHE9 4.8 36.9 1.0 CB A:ASN17 4.8 50.7 1.0 CA A:CYS21 4.8 65.3 1.0 O A:PHE23 4.9 57.9 1.0

Cadmium binding site 2 out of 4 in the Hrsv M2-1, P422 Crystal Form


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of Hrsv M2-1, P422 Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd301 b:49.9 occ:1.00 O A:HOH2021 2.2 64.8 1.0 O A:HOH2020 2.3 47.6 1.0 ND1 A:HIS14 2.3 43.0 1.0 OE1 A:GLU10 2.5 39.2 1.0 OE2 A:GLU10 2.6 38.6 1.0 O A:HOH2018 2.8 42.1 1.0 O A:HOH2039 2.8 47.6 1.0 CD A:GLU10 2.9 38.6 1.0 CE1 A:HIS14 3.1 41.2 1.0 CG A:HIS14 3.5 42.0 1.0 CB A:HIS14 3.9 39.9 1.0 CA A:HIS14 3.9 43.3 1.0 OH A:TYR27 4.1 36.5 1.0 NE2 A:HIS14 4.3 35.8 1.0 CG A:GLU10 4.4 32.0 1.0 N A:CYS15 4.4 45.8 1.0 CD2 A:HIS14 4.5 38.4 1.0 O A:GLY13 4.5 34.8 1.0 C A:HIS14 4.7 38.6 1.0 NH2 A:ARG38 4.8 34.5 1.0

Cadmium binding site 3 out of 4 in the Hrsv M2-1, P422 Crystal Form


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 3 of Hrsv M2-1, P422 Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cd201 b:51.0 occ:1.00 NE2 B:HIS25 2.2 60.3 1.0 SG B:CYS15 2.2 45.1 1.0 SG B:CYS21 2.5 58.6 1.0 SG B:CYS7 2.7 47.7 1.0 CE1 B:HIS25 3.0 61.2 1.0 CB B:CYS15 3.2 47.0 1.0 CD2 B:HIS25 3.3 57.3 1.0 CB B:CYS21 3.3 60.0 1.0 CB B:CYS7 3.4 42.9 1.0 ND1 B:HIS25 4.2 53.3 1.0 CG B:HIS25 4.3 50.0 1.0 CA B:CYS15 4.6 43.0 1.0 CA B:CYS21 4.8 59.9 1.0 CB B:PHE23 4.8 54.4 1.0 CA B:CYS7 4.8 41.5 1.0 CB B:ASN17 4.8 55.4 1.0 O B:PHE23 4.9 52.5 1.0 CB B:PHE9 4.9 47.9 1.0 CD2 B:PHE9 4.9 51.4 1.0

Cadmium binding site 4 out of 4 in the Hrsv M2-1, P422 Crystal Form


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 4 of Hrsv M2-1, P422 Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cd301 b:56.6 occ:1.00 ND1 B:HIS14 2.3 46.5 1.0 OE1 B:GLU10 2.6 43.9 1.0 OE2 B:GLU10 2.7 43.3 1.0 O B:HOH2012 2.7 54.9 1.0 O B:HOH2009 2.8 63.7 1.0 O B:HOH2010 2.8 66.8 1.0 CD B:GLU10 3.0 44.0 1.0 CE1 B:HIS14 3.0 45.0 1.0 O B:HOH2011 3.2 61.9 1.0 CG B:HIS14 3.5 42.2 1.0 CB B:HIS14 4.0 42.2 1.0 OH B:TYR27 4.0 41.1 1.0 CA B:HIS14 4.1 49.5 1.0 NE2 B:HIS14 4.2 41.1 1.0 CG B:GLU10 4.4 44.3 1.0 CD2 B:HIS14 4.5 37.6 1.0 N B:CYS15 4.6 44.4 1.0 O B:GLY13 4.6 46.6 1.0 C B:HIS14 4.8 44.0 1.0 NH2 B:ARG38 4.9 44.5 1.0

S.J.Tanner, A.Ariza, C.Richard, H.F.Kyle, R.L.Dods, M.Blondot, W.Wu, J.Trincao, C.H.Trinh, J.A.Hiscox, M.W.Carroll, N.J.Silman, J.Eleouet, T.A.Edwards, J.N.Barr. Crystal Structure of the Essential Transcription Antiterminator M2-1 Protein of Human Respiratory Syncytial Virus and Implications of Its Phosphorylation. Proc.Natl.Acad.Sci.Usa V. 111 1580 2014.
ISSN: ISSN 0027-8424
PubMed: 24434552
DOI: 10.1073/PNAS.1317262111